Publications of Daniel P Kiehart :chronological combined listing:
%% Papers Published
@article{fds153494,
Author = {Y Toyama and XG Peralta and AR Wells and DP Kiehart and GS
Edwards},
Title = {Apoptotic force and tissue dynamics during Drosophila
embryogenesis.},
Journal = {Science (New York, N.Y.), United States},
Volume = {321},
Number = {5896},
Pages = {1683-6},
Year = {2008},
Month = {September},
Keywords = {Animals • Apoptosis* • Cell Movement • Cell
Shape • Drosophila melanogaster • Embryo,
Nonmammalian • Embryonic Development* • Epidermis
• Epithelial Cells • Epithelium • Female
• Microscopy, Confocal • Morphogenesis* •
cytology • cytology* • embryology •
embryology* • physiology},
Abstract = {Understanding cell morphogenesis during metazoan development
requires knowledge of how cells and the extracellular matrix
produce and respond to forces. We investigated how
apoptosis, which remodels tissue by eliminating
supernumerary cells, also contributes forces to a tissue
(the amnioserosa) that promotes cell-sheet fusion (dorsal
closure) in the Drosophila embryo. We showed that expression
in the amnioserosa of proteins that suppress or enhance
apoptosis slows or speeds dorsal closure, respectively.
These changes correlate with the forces produced by the
amnioserosa and the rate of seam formation between the cell
sheets (zipping), key processes that contribute to closure.
This apoptotic force is used by the embryo to drive
cell-sheet movements during development, a role not
classically attributed to apoptosis.},
Key = {fds153494}
}
@article{fds148186,
Author = {A Rodriguez-Diaz and Y Toyama and DL Abravanel and JM Wiemann and AR
Wells, US Tulu and GS Edwards and DP Kiehart.},
Title = {Actomyosin purse strings: renewable resources that make
morphogenesis robust and resilient.},
Journal = {HFSP J.},
Volume = {2},
Number = {4},
Pages = {220-237},
Year = {2008},
Key = {fds148186}
}
@article{fds148184,
Author = {XG Peralta and Y Toyama and DP Kiehart and GS Edwards},
Title = {Emergent properties during dorsal closure in Drosophila
morphogenesis.},
Journal = {Physical biology, England},
Volume = {5},
Number = {1},
Pages = {15004},
Year = {2008},
ISSN = {1478-3975},
Keywords = {Actins • Animals • Animals, Genetically Modified
• Biomechanics • Drosophila melanogaster •
Embryo, Nonmammalian • Embryonic Development •
Epidermis • Gene Expression Regulation, Developmental
• Green Fluorescent Proteins • Image Processing,
Computer-Assisted • Microscopy, Confocal •
Microscopy, Fluorescence • Recombinant Fusion Proteins
• anatomy & histology • cytology • embryology
• embryology* • genetics • metabolism •
physiology • physiology*},
Abstract = {Dorsal closure is an essential stage of Drosophila
development that is a model system for research in
morphogenesis and biological physics. Dorsal closure
involves an orchestrated interplay between gene expression
and cell activities that produce shape changes, exert forces
and mediate tissue dynamics. We investigate the dynamics of
dorsal closure based on confocal microscopic measurements of
cell shortening in living embryos. During the mid-stages of
dorsal closure we find that there are fluctuations in the
width of the leading edge cells but the time-averaged
analysis of measurements indicate that there is essentially
no net shortening of cells in the bulk of the leading edge,
that contraction predominantly occurs at the canthi as part
of the process for zipping together the two leading edges of
epidermis and that the rate constant for zipping correlates
with the rate of movement of the leading edges. We
characterize emergent properties that regulate dorsal
closure, i.e., a velocity governor and the coordination and
synchronization of tissue dynamics.},
Key = {fds148184}
}
@article{fds148185,
Author = {SV Todi and E Sivan-Loukianova and JS Jacobs and DP Kiehart and DF
Eberl},
Title = {Myosin VIIA, important for human auditory function, is
necessary for Drosophila auditory organ development.},
Journal = {PLoS ONE, United States},
Volume = {3},
Number = {5},
Pages = {e2115},
Year = {2008},
ISSN = {1932-6203},
Keywords = {Animals • Auditory Perception • Conserved Sequence
• Drosophila • Drosophila Proteins • Dynein
ATPase • Evolution, Molecular • Humans •
Mutation • Myosins • Sensory Receptor Cells •
genetics • physiology • physiology*},
Abstract = {BACKGROUND: Myosin VIIA (MyoVIIA) is an unconventional
myosin necessary for vertebrate audition [1]-[5]. Human
auditory transduction occurs in sensory hair cells with a
staircase-like arrangement of apical protrusions called
stereocilia. In these hair cells, MyoVIIA maintains
stereocilia organization [6]. Severe mutations in the
Drosophila MyoVIIA orthologue, crinkled (ck), are
semi-lethal [7] and lead to deafness by disrupting antennal
auditory organ (Johnston's Organ, JO) organization [8].
ck/MyoVIIA mutations result in apical detachment of auditory
transduction units (scolopidia) from the cuticle that
transmits antennal vibrations as mechanical stimuli to JO.
PRINCIPAL FINDINGS: Using flies expressing GFP-tagged NompA,
a protein required for auditory organ organization in
Drosophila, we examined the role of ck/MyoVIIA in JO
development and maintenance through confocal microscopy and
extracellular electrophysiology. Here we show that
ck/MyoVIIA is necessary early in the developing antenna for
initial apical attachment of the scolopidia to the
articulating joint. ck/MyoVIIA is also necessary to maintain
scolopidial attachment throughout adulthood. Moreover, in
the adult JO, ck/MyoVIIA genetically interacts with the
non-muscle myosin II (through its regulatory light chain
protein and the myosin binding subunit of myosin II
phosphatase). Such genetic interactions have not previously
been observed in scolopidia. These factors are therefore
candidates for modulating MyoVIIA activity in vertebrates.
CONCLUSIONS: Our findings indicate that MyoVIIA plays
evolutionarily conserved roles in auditory organ development
and maintenance in invertebrates and vertebrates, enhancing
our understanding of auditory organ development and
function, as well as providing significant clues for future
research.},
Key = {fds148185}
}
@article{fds143471,
Author = {JD Franke and RA Montague and WL Rickoll and DP Kiehart},
Title = {An MYH9 human disease model in flies: site-directed
mutagenesis of the Drosophila non-muscle myosin II results
in hypomorphic alleles with dominant character.},
Journal = {Human molecular genetics, England},
Volume = {16},
Number = {24},
Pages = {3160-73},
Year = {2007},
Month = {December},
ISSN = {0964-6906},
Keywords = {Alleles • Amino Acid Sequence • Animals •
Animals, Genetically Modified • Blood Platelet
Disorders • Crosses, Genetic • Disease Models,
Animal* • Drosophila • Drosophila Proteins •
Genes, Dominant* • Humans • Membrane Proteins
• Models, Biological • Molecular Motor Proteins
• Molecular Sequence Data • Mutagenesis,
Site-Directed* • Myosin Heavy Chains • Phenotype
• Sequence Homology, Amino Acid • Transgenes
• genetics • genetics* • pathology},
Abstract = {We investigated whether or not human disease-causing, amino
acid substitutions in MYH9 could cause dominant phenotypes
when introduced into the sole non-muscle myosin II heavy
chain in Drosophila melanogaster (zip/MyoII). We
characterized in vivo the effects of four MYH9-like
mutations in the myosin rod-R1171C, D1430N, D1847K and
R1939X-which occur at highly conserved residues. These
engineered mutant heavy chains resulted in D. melanogaster
non-muscle myosin II with partial wild-type function. In a
wild-type genetic background, mutant heavy chains were
overtly recessive and hypomorphic: each was able to
substitute partially for endogenous non-muscle myosin II
heavy chain in animals lacking zygotically produced heavy
chain (but the penetrance of rescue was below Mendelian
expectation). Moreover, each of the four mutant heavy chains
exhibits dominant characteristics when expressed in a
sensitized genetic background (flies heterozygous for RhoA
mutations). Thus, these zip/MyoII(MYH9) alleles function,
like certain other hypomorphic alleles, as excellent bait in
screens for genetic interactors. Our conjecture is that
these mutations in D. melanogaster behave comparably to
their parent mutations in humans. We further characterized
these zip/MyoII(MYH9) alleles, and found that all were
capable of correct spatial and temporal localization in
animals lacking zygotic expression of wild-type zip/MyoII.
In vitro, we demonstrate that mutant heavy chains can
dimerize with endogenous, wild-type heavy chains, fold into
coiled-coil structures and assemble into higher-order
structures. Our work further supports D. melanogaster as a
model system for investigating the basis of human
disease.},
Key = {fds143471}
}
@article{fds143472,
Author = {XG Peralta and Y Toyama and MS Hutson and R Montague and S Venakides and DP
Kiehart, GS Edwards},
Title = {Upregulation of forces and morphogenic asymmetries in dorsal
closure during Drosophila development.},
Journal = {Biophysical journal, United States},
Volume = {92},
Number = {7},
Pages = {2583-96},
Year = {2007},
Month = {April},
ISSN = {0006-3495},
Keywords = {Animals • Computer Simulation • Drosophila •
Mechanotransduction, Cellular • Models, Biological*
• Morphogenesis • Stress, Mechanical •
Up-Regulation • anatomy & histology • embryology*
• physiology • physiology*},
Abstract = {Tissue dynamics during dorsal closure, a stage of Drosophila
development, provide a model system for cell sheet
morphogenesis and wound healing. Dorsal closure is
characterized by complex cell sheet movements, driven by
multiple tissue specific forces, which are coordinated in
space, synchronized in time, and resilient to UV-laser
perturbations. The mechanisms responsible for these
attributes are not fully understood. We measured spatial,
kinematic, and dynamic antero-posterior asymmetries to
biophysically characterize both resiliency to laser
perturbations and failure of closure in mutant embryos and
compared them to natural asymmetries in unperturbed,
wild-type closure. We quantified and mathematically modeled
two processes that are upregulated to provide
resiliency--contractility of the amnioserosa and formation
of a seam between advancing epidermal sheets, i.e., zipping.
Both processes are spatially removed from the laser-targeted
site, indicating they are not a local response to
laser-induced wounding and suggesting mechanosensitive
and/or chemosensitive mechanisms for upregulation. In mutant
embryos, tissue junctions initially fail at the anterior end
indicating inhomogeneous mechanical stresses attributable to
head involution, another developmental process that occurs
concomitant with the end stages of closure. Asymmetries in
these mutants are reversed compared to wild-type, and
inhomogeneous stresses may cause asymmetries in wild-type
closure.},
Key = {fds143472}
}
@article{fds143474,
Author = {D.P. Kiehart and K. Bloom},
Title = {Cell structure and dynamics},
Journal = {Current Opinion in Cell Biology},
Volume = {19},
Number = {1},
Pages = {1-4},
Editor = {D.P. Kiehart and K. Bloom},
Year = {2007},
Month = {February},
Key = {fds143474}
}
@article{fds52024,
Author = {JD Franke and AL Boury and NJ Gerald and DP Kiehart},
Title = {Native nonmuscle myosin II stability and light chain binding
in Drosophila melanogaster.},
Journal = {Cell motility and the cytoskeleton, United
States},
Volume = {63},
Number = {10},
Pages = {604-22},
Year = {2006},
Month = {October},
Keywords = {Amino Acid Sequence • Animals • Animals,
Genetically Modified • Drosophila melanogaster •
Dynein ATPase • Fluorescent Antibody Technique •
Immunoprecipitation • Mass Spectrometry •
Molecular Sequence Data • Mutation • Myosin Heavy
Chains • Myosin Light Chains • Myosin Type II
• Myosin Type V • Myosins • Sequence
Homology, Amino Acid • genetics • metabolism
• metabolism*},
Abstract = {Native nonmuscle myosin IIs play essential roles in cellular
and developmental processes throughout phylogeny. Individual
motor molecules consist of a heterohexameric complex of
three polypeptides which, when properly assembled, are
capable of force generation. Here, we more completely
characterize the properties, relationships and associations
that each subunit has with one another in Drosophila
melanogaster. All three native nonmuscle myosin II
polypeptide subunits are expressed in close to constant
stoichiometry to each other throughout development. We find
that the stability of two subunits, the heavy chain and the
regulatory light chain, depend on one another whereas the
stability of the third subunit, the essential light chain,
does not depend on either the heavy chain or regulatory
light chain. We demonstrate that heavy chain aggregates,
which form when regulatory light chain is lacking, associate
with the essential light chain in vivo-thus showing that
regulatory light chain association is required for heavy
chain solubility. By immunodepletion we find that the
majority of both light chains are associated with the
nonmuscle myosin II heavy chain but pools of free light
chain and/or light chain bound to other proteins are
present. We identify four myosins (myosin II, myosin V,
myosin VI and myosin VIIA) and a microtubule-associated
protein (asp/Abnormal spindle) as binding partners for the
essential light chain (but not the regulatory light chain)
through mass spectrometry and co-precipitation. Using an in
silico approach we identify six previously uncharacterized
genes that contain IQ-motifs and may be essential light
chain binding partners.},
Key = {fds52024}
}
@article{fds52164,
Author = {Y Yang and M Kovács and T Sakamoto and F Zhang and DP Kiehart, JR
Sellers},
Title = {Dimerized Drosophila myosin VIIa: a processive
motor.},
Journal = {Proceedings of the National Academy of Sciences of the
United States of America, United States},
Volume = {103},
Number = {15},
Pages = {5746-51},
Year = {2006},
Month = {April},
Keywords = {Animals • DNA, Complementary • Dimerization •
Drosophila • Drosophila Proteins • Dynein ATPase
• Kinetics • Myosins • Recombinant Fusion
Proteins • chemistry • enzymology* • genetics
• metabolism • metabolism*},
Abstract = {The molecular mechanism of processive movement of single
myosin molecules from classes V and VI along their actin
tracks has recently attracted extraordinary attention.
Another member of the myosin superfamily, myosin VII, plays
vital roles in the sensory function of Drosophila and
mammals. We studied the molecular mechanism of Drosophila
myosin VIIa, using transient kinetics and single-molecule
motility assays. Myosin VIIa moves along actin filaments as
a processive, double-headed single molecule when dimerized
by the inclusion of a leucine zipper at the C terminus of
the coiled-coil domain. Its motility is approximately 8-10
times slower than that of myosin V, and its step size is 30
nm, which is consistent with the presence of five IQ motifs
in its neck region. The kinetic basis for the processive
motility of myosin VIIa is the relative magnitude of the
release rate constants of phosphate (fast) and ADP (slow) as
in myosins V and VI. The ATPase pathway is rate-limited by a
reversible interconversion between two distinct ADP-bound
actomyosin states, which results in high steady-state
occupancy of a strongly actin-bound myosin species. The
distinctive features of myosin VIIa (long run lengths, slow
motility) will be very useful in video-based single-molecule
applications. In cells, this kinetic behavior would allow
myosin VIIa to exert and hold tension on actin filaments
and, if dimerized, to function as a processive cargo
transporter.},
Key = {fds52164}
}
@article{fds44747,
Author = {JG Homsy and H Jasper and XG Peralta and H Wu and DP Kiehart and D
Bohmann},
Title = {JNK signaling coordinates integrin and actin functions
during Drosophila embryogenesis.},
Journal = {Developmental dynamics : an official publication of the
American Association of Anatomists, United
States},
Volume = {235},
Number = {2},
Pages = {427-34},
Year = {2006},
Month = {February},
Keywords = {Actins • Animals • Drosophila melanogaster •
Embryonic Development* • Gene Expression Regulation,
Developmental • Integrins • JNK Mitogen-Activated
Protein Kinases • Mutation • Signal Transduction*
• embryology* • genetics •
metabolism*},
Abstract = {Epithelial movements are key morphogenetic events in animal
development. They are driven by multiple mechanisms,
including signal-dependent changes in cytoskeletal
organization and in cell adhesion. Such processes must be
controlled precisely and coordinated to accurately sculpt
the three-dimensional form of the developing organism. By
observing the Drosophila epidermis during embryonic
development using confocal time-lapse microscopy, we have
investigated how signaling through the Jun-N-terminal kinase
(JNK) pathway governs the tissue sheet movements that result
in dorsal closure (DC). We find that JNK controls the
polymerization of actin into a cable at the epidermal
leading edge as previously suggested, as well as the joining
(zipping) of the contralateral epithelial cell sheets. Here,
we show that zipping is mediated by regulation of the
integrins myospheroid and scab. Our data demonstrate that
JNK signaling regulates a set of target genes that cooperate
to facilitate epithelial movement and closure.},
Key = {fds44747}
}
@article{fds44753,
Author = {DP Kiehart and Y Tokutake and MS Chang and MS Hutson and J Wiemann and XG
Peralta, Y Toyama and AR Wells and ARogriguez, GS
Edwards},
Title = {Ultraviolet Laser Microbeam for Dissection of Drosophila
Embryos},
Series = {3rd edition},
Pages = {87-103},
Booktitle = {Cell Biology: A Laboratory Handbook},
Publisher = {Elsevier},
Editor = {J.E. Celis},
Year = {2006},
Key = {fds44753}
}
@article{fds44746,
Author = {JD Franke and RA Montague and DP Kiehart},
Title = {Nonmuscle myosin II generates forces that transmit tension
and drive contraction in multiple tissues during dorsal
closure.},
Journal = {Current biology : CB, England},
Volume = {15},
Number = {24},
Pages = {2208-21},
Year = {2005},
Month = {December},
Keywords = {Amino Acid Sequence • Animals • Animals,
Genetically Modified • Base Sequence •
Biomechanics • Body Patterning • Cytoskeleton
• Drosophila • Drosophila Proteins • Embryo,
Nonmammalian • Green Fluorescent Proteins •
Membrane Proteins • Microscopy, Confocal •
Molecular Sequence Data • Morphogenesis • Myosin
Heavy Chains • Myosin Type II • Sequence Analysis,
DNA • cytology • embryology* • genetics
• metabolism • physiology •
physiology*},
Abstract = {BACKGROUND: The morphogenic movements that characterize
embryonic development require the precise temporal and
spatial control of cell-shape changes. Drosophila dorsal
closure is a well-established model for epithelial sheet
morphogenesis, and mutations in more than 60 genes cause
defects in closure. Closure requires that four forces,
derived from distinct tissues, be precisely balanced. The
proteins responsible for generating each of the forces have
not been determined. RESULTS: We document dorsal closure in
living embryos to show that mutations in nonmuscle myosin II
(encoded by zipper; zip/MyoII) disrupt the integrity of
multiple tissues during closure. We demonstrate that MyoII
localization is distinct from, but overlaps, F-actin in the
supracellular purse string, whereas in the amnioserosa and
lateral epidermis each has similar, cortical distributions.
In zip/MyoII mutant embryos, we restore MyoII function
either ubiquitously or specifically in the leading edge,
amnioserosa, or lateral epidermis and find that zip/MyoII
function in any one tissue can rescue closure. Using a
novel, transgenic mosaic approach, we establish that
contractility of the supracellular purse string in
leading-edge cells requires zip/MyoII-generated forces; that
zip/MyoII function is responsible for the apical contraction
of amnioserosa cells; that zip/MyoII is important for
zipping; and that defects in zip/MyoII contractility cause
the misalignment of the lateral-epidermal sheets during seam
formation. CONCLUSIONS: We establish that zip/MyoII is
responsible for generating the forces that drive cell-shape
changes in each of the force-generating tissues that
contribute to closure. This highly conserved contractile
protein likely drives cell-sheet movements throughout
phylogeny.},
Key = {fds44746}
}
@article{fds44748,
Author = {SV Todi and JD Franke and DP Kiehart and DF Eberl},
Title = {Myosin VIIA defects, which underlie the Usher 1B syndrome in
humans, lead to deafness in Drosophila.},
Journal = {Current biology : CB, England},
Volume = {15},
Number = {9},
Pages = {862-8},
Year = {2005},
Month = {May},
Keywords = {Animals • Cloning, Molecular • Deafness •
Drosophila • Dynein ATPase • Ear, Inner •
Electrophysiology • Evoked Potentials, Auditory •
Hair Cells, Auditory • Humans •
Immunohistochemistry • Intercellular Junctions •
Microscopy, Confocal • Mutation • Myosins •
Signal Transduction • genetics • genetics* •
metabolism* • physiology • physiology*},
Abstract = {In vertebrates, auditory and vestibular transduction occurs
on apical projections (stereocilia) of specialized cells
(hair cells). Mutations in myosin VIIA (myoVIIA), an
unconventional myosin, lead to deafness and balance
anomalies in humans, mice, and zebrafish; individuals are
deaf, and stereocilia are disorganized. The exact mechanism
through which myoVIIA mutations result in these inner-ear
anomalies is unknown. Proposed inner-ear functions for
myoVIIA include anchoring transduction channels to the
stereocilia membrane, trafficking stereocilia linking
components, and anchoring hair cells by associating with
adherens junctions. The Drosophila myoVIIA homolog is
crinkled (ck). The Drosophila auditory organ, Johnston's
organ (JO), is developmentally and functionally related to
the vertebrate inner ear. Both derive from modified
epithelial cells specified by atonal and spalt homolog
expression, and both transduce acoustic mechanical energy
(and references therein). Here, we show that loss of
ck/myoVIIA function leads to complete deafness in Drosophila
by disrupting the integrity of the scolopidia that transduce
auditory signals. We demonstrate that ck/myoVIIA functions
to organize the auditory organ, that it is functionally
required in neuronal and support cells, that it is not
required for TRPV channel localization, and that it is not
essential for scolopidial-cell-junction integrity.},
Key = {fds44748}
}
@article{fds30404,
Author = {JD Franke and F Dong and WL Rickoll and MJ Kelley and DP
Kiehart},
Title = {Rod mutations associated with MYH9-related disorders disrupt
nonmuscle myosin-IIA assembly.},
Journal = {Blood, United States},
Volume = {105},
Number = {1},
Pages = {161-9},
Year = {2005},
Month = {January},
Keywords = {Circular Dichroism • DNA Glycosylases •
Microscopy, Electron • Mutation • Nonmuscle Myosin
Type IIA • Retinal Rod Photoreceptor Cells • Salts
• Temperature • chemistry* • genetics* •
metabolism* • pharmacology • ultrastructure},
Abstract = {MYH9-related disorders are autosomal dominant syndromes,
variably affecting platelet formation, hearing, and kidney
function, and result from mutations in the human nonmuscle
myosin-IIA heavy chain gene. To understand the mechanisms by
which mutations in the rod region disrupt nonmuscle
myosin-IIA function, we examined the in vitro behavior of 4
common mutant forms of the rod (R1165C, D1424N, E1841K, and
R1933Stop) compared with wild type. We used negative-stain
electron microscopy to analyze paracrystal morphology, a
model system for the assembly of individual myosin-II
molecules into bipolar filaments. Wild-type tail fragments
formed ordered paracrystal arrays, whereas mutants formed
aberrant aggregates. In mixing experiments, the mutants act
dominantly to interfere with the proper assembly of wild
type. Using circular dichroism, we find that 2 mutants
affect the alpha-helical coiled-coil structure of individual
molecules, and 2 mutants disrupt the lateral associations
among individual molecules necessary to form higher-order
assemblies, helping explain the dominant effects of these
mutants. These results demonstrate that the most common
mutations in MYH9, lesions in the rod, cause defects in
nonmuscle myosin-IIA assembly. Further, the application of
these methods to biochemically characterize rod mutations
could be extended to other myosins responsible for
disease.},
Key = {fds30404}
}
@article{fds30401,
Author = {DP Kiehart and JD Franke and MK Chee and RA Montague and TL Chen and J
Roote, M Ashburner},
Title = {Drosophila crinkled, mutations of which disrupt
morphogenesis and cause lethality, encodes fly myosin
VIIA.},
Journal = {Genetics, United States},
Volume = {168},
Number = {3},
Pages = {1337-52},
Year = {2004},
Month = {November},
Keywords = {Amino Acid Sequence • Animals • Conserved Sequence
• Drosophila melanogaster • Dynein ATPase •
Genes, Lethal • Models, Molecular • Molecular
Sequence Data • Mutation • Myosins •
Phenotype • Protein Structure, Tertiary • Sequence
Analysis, Protein • genetics* •
metabolism},
Abstract = {Myosin VIIs provide motor function for a wide range of
eukaryotic processes. We demonstrate that mutations in
crinkled (ck) disrupt the Drosophila myosin VIIA heavy
chain. The ck/myoVIIA protein is present at a low level
throughout fly development and at the same level in heads,
thoraxes, and abdomens. Severe ck alleles, likely to be
molecular nulls, die as embryos or larvae, but all allelic
combinations tested thus far yield a small fraction of adult
"escapers" that are weak and infertile. Scanning electron
microscopy shows that escapers have defects in bristles and
hairs, indicating that this motor protein plays a role in
the structure of the actin cytoskeleton. We generate a
homology model for the structure of the ck/myosin VIIA head
that indicates myosin VIIAs, like myosin IIs, have a
spectrin-like, SH3 subdomain fronting their N terminus. In
addition, we establish that the two myosin VIIA FERM repeats
share high sequence similarity with only the first two
subdomains of the three-lobed structure that is typical of
canonical FERM domains. Nevertheless, the approximately 100
and approximately 75 amino acids that follow the first two
lobes of the first and second FERM domains are highly
conserved among myosin VIIs, suggesting that they compose a
conserved myosin tail homology 7 (MyTH7) domain that may be
an integral part of the FERM domain or may function
independently of it. Together, our data suggest a key role
for ck/myoVIIA in the formation of cellular projections and
other actin-based functions required for
viability.},
Key = {fds30401}
}
@article{fds30403,
Author = {JB Dorman and KE James and SE Fraser and DP Kiehart and CA
Berg},
Title = {bullwinkle is required for epithelial morphogenesis during
Drosophila oogenesis.},
Journal = {Developmental biology, United States},
Volume = {267},
Number = {2},
Pages = {320-41},
Year = {2004},
Month = {March},
url = {http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract&list_uids=15013797},
Keywords = {Animals • Drosophila Proteins • Drosophila
melanogaster • Epithelium • Fluorescent Antibody
Technique • Gene Expression Regulation, Developmental*
• Membrane Proteins • Microscopy, Confocal •
Morphogenesis • Oogenesis • Transcription Factors
• beta-Galactosidase • embryology •
embryology* • metabolism • physiology*},
Abstract = {Many organs, such as the liver, neural tube, and lung, form
by the precise remodeling of flat epithelial sheets into
tubes. Here we investigate epithelial tubulogenesis in
Drosophila melanogaster by examining the development of the
dorsal respiratory appendages of the eggshell. We employ a
culture system that permits confocal analysis of stage 10-14
egg chambers. Time-lapse imaging of GFP-Moesin-expressing
egg chambers reveals three phases of morphogenesis: tube
formation, anterior extension, and paddle maturation. The
dorsal-appendage-forming cells, previously thought to
represent a single cell fate, consist of two subpopulations,
those forming the tube roof and those forming the tube
floor. These two cell types exhibit distinct morphological
and molecular features. Roof-forming cells constrict
apically and express high levels of Broad protein. Floor
cells lack Broad, express the rhomboid-lacZ marker, and form
the floor by directed cell elongation. We examine the
morphogenetic phenotype of the bullwinkle (bwk) mutant and
identify defects in both roof and floor formation. Dorsal
appendage formation is an excellent system in which cell
biological, molecular, and genetic tools facilitate the
study of epithelial morphogenesis.},
Key = {fds30403}
}
@article{fds153495,
Author = {DP Kiehart},
Title = {Myosins motor Miranda.},
Journal = {Molecular cell, United States},
Volume = {12},
Number = {6},
Pages = {1346-7},
Year = {2003},
Month = {December},
Keywords = {Animals • Cell Cycle Proteins • Cell Division
• Cell Polarity • Drosophila Proteins •
Drosophila melanogaster • Membrane Proteins •
Myosin Heavy Chains • cytology • embryology •
genetics • metabolism • metabolism* •
physiology},
Abstract = {New evidence shows that myosin motors drive the spatial
segregation of cell fate determinants during asymmetric cell
division. How they do so remains a mystery.},
Key = {fds153495}
}
@article{fds153496,
Author = {CA Bayer, SR Halsell and JW Fristrom and DP Kiehart and L von
Kalm},
Title = {Genetic interactions between the RhoA and Stubble-stubbloid
loci suggest a role for a type II transmembrane serine
protease in intracellular signaling during Drosophila
imaginal disc morphogenesis.},
Journal = {Genetics, United States},
Volume = {165},
Number = {3},
Pages = {1417-32},
Year = {2003},
Month = {November},
Keywords = {Animals • Cloning, Molecular • Drosophila •
Drosophila Proteins • Gene Dosage • Membrane
Proteins • Morphogenesis • Mutation • Serine
Endopeptidases • Signal Transduction* • Transgenes
• genetics* • growth & development •
metabolism* • rhoA GTP-Binding Protein},
Abstract = {The Drosophila RhoA (Rho1) GTPase is essential for
postembryonic morphogenesis of leg and wing imaginal discs.
Mutations in RhoA enhance leg and wing defects associated
with mutations in zipper, the gene encoding the heavy chain
of nonmuscle myosin II. We demonstrate here that mutations
affecting the RhoA signaling pathway also interact
genetically with mutations in the Stubble-stubbloid (Sb-sbd)
locus that encodes an unusual type II transmembrane serine
protease required for normal leg and wing morphogenesis. In
addition, a leg malformation phenotype associated with
overexpression of Sb-sbd in prepupal leg discs is suppressed
when RhoA gene dose is reduced, suggesting that RhoA and
Sb-sbd act in a common pathway during leg morphogenesis. We
also characterized six mutations identified as enhancers of
zipper mutant leg defects. Three of these genes encode known
members of the RhoA signaling pathway (RhoA, DRhoGEF2, and
zipper). The remaining three enhancer of zipper mutations
interact genetically with both RhoA and Sb-sbd mutations,
suggesting that they encode additional components of the
RhoA signaling pathway in imaginal discs. Our results
provide evidence that the type II transmembrane serine
proteases, a class of proteins linked to human developmental
abnormalities and pathology, may be associated with
intracellular signaling required for normal
development.},
Key = {fds153496}
}
@article{fds153497,
Author = {MS Hutson and Y Tokutake and MS Chang and JW Bloor and S Venakides and DP
Kiehart, GS Edwards},
Title = {Forces for morphogenesis investigated with laser
microsurgery and quantitative modeling.},
Journal = {Science (New York, N.Y.), United States},
Volume = {300},
Number = {5616},
Pages = {145-9},
Year = {2003},
Month = {April},
Keywords = {Animals • Animals, Genetically Modified • Cell
Adhesion • Drosophila • Drosophila Proteins •
Embryo, Nonmammalian • Embryonic Development •
Epithelial Cells • Epithelium • Genes, Insect
• Image Processing, Computer-Assisted • Integrin
alpha Chains • Integrins • Lasers •
Mathematics • Microscopy, Confocal • Microsurgery
• Models, Biological* • Morphogenesis* •
Mutation • Pseudopodia • embryology* •
genetics • physiology • physiology*},
Abstract = {We investigated the forces that connect the genetic program
of development to morphogenesis in Drosophila. We focused on
dorsal closure, a powerful model system for development and
wound healing. We found that the bulk of progress toward
closure is driven by contractility in supracellular "purse
strings" and in the amnioserosa, whereas adhesion-mediated
zipping coordinates the forces produced by the purse strings
and is essential only for the end stages. We applied
quantitative modeling to show that these forces, generated
in distinct cells, are coordinated in space and synchronized
in time. Modeling of wild-type and mutant phenotypes is
predictive; although closure in myospheroid mutants
ultimately fails when the cell sheets rip themselves apart,
our analysis indicates that beta(PS) integrin has an
earlier, important role in zipping.},
Key = {fds153497}
}
@article{fds16942,
Author = {Hutson, M.S. and Y.Tokutake, M-S. Chang and J.W. Bloor and S.Venakides, D.P.Kiehart and G.S.Edwards.},
Title = {Forces for Morphogenesis Investigated with Laser
Microsurgery and Quantitative Modeling},
Journal = {Science},
Volume = {300},
Pages = {145-149},
Year = {2003},
Key = {fds16942}
}
@article{fds16943,
Author = {Bayer, C.A. and S.R.Halsell, J.W.Fristrom and D.P.Kiehart and L.von Kalm. 2003. Genetic interactions between the RhoA and Stubble-stubbloid loci suggest a role for a Type II
Transmembrane Serine Protease in intracellular signaling
during Drosophila imaginal di},
Title = {Genetic interactions between the RhoA and Stubble-stubbloid
loci suggest a role for a Type II Transmembrane Serine
Protease in intracellular signaling during Drosophila
imaginal disc morphogenesis},
Journal = {Genetics},
Volume = {165},
Pages = {1417-1432},
Year = {2003},
Key = {fds16943}
}
@article{fds16946,
Author = {G.S. Edwards and R.H. Austin and F.E. Carroll and M.L. Copeland and M.E.
Couprie, W.E.Gabella and R.F. Haglund and B.A. Hooper and M.S.
Hutson, E.D. Jansen and K.M. Joos and D.P. Kiehart and I. Lindau and J.
Miao, H.S. Pratisto and J.H. Shen and Y. Tokutake and L. van der
Meer and A. Xie},
Title = {FEL-based-biophysical and biomedical instrumentation},
Journal = {Review of Scientific Instruments},
Volume = {74},
Pages = {3207-3245},
Year = {2003},
Key = {fds16946}
}
@article{fds16948,
Author = {D.P. Kiehart},
Title = {Myosins Motor Miranda},
Journal = {Molecular Cell},
Volume = {12},
Pages = {1346-1347},
Year = {2003},
Key = {fds16948}
}
@article{fds153499,
Author = {DP Kiehart and JD Franke},
Title = {Actin dynamics: the arp2/3 complex branches
out.},
Journal = {Current biology : CB, England},
Volume = {12},
Number = {16},
Pages = {R557-9},
Year = {2002},
Month = {August},
Keywords = {Actin-Related Protein 2 • Actin-Related Protein 3
• Actins • Animals • Contractile Proteins*
• Cytoskeletal Proteins • Cytoskeleton •
Drosophila Proteins • Drosophila melanogaster •
Embryo, Nonmammalian • Macromolecular Substances •
Microfilament Proteins • Oocytes • Oogenesis
• Profilins • cytology • genetics •
metabolism • metabolism* • physiology},
Abstract = {Several new findings point to novel functions for the Arp2/3
complex. The dendritic nucleation model that has been
proposed to describe cell extension for locomotion may also
be applicable to other actin-based processes.},
Key = {fds153499}
}
@article{fds153500,
Author = {JW Bloor and DP Kiehart},
Title = {Drosophila RhoA regulates the cytoskeleton and cell-cell
adhesion in the developing epidermis.},
Journal = {Development (Cambridge, England), England},
Volume = {129},
Number = {13},
Pages = {3173-83},
Year = {2002},
Month = {July},
Keywords = {Actomyosin • Animals • Animals, Genetically
Modified • Cadherins • Cell Adhesion • Cell
Polarity • Cytoskeleton • Drosophila •
Embryo, Nonmammalian • Epidermis • Female •
Gene Expression Regulation, Developmental • Genes,
Dominant • JNK Mitogen-Activated Protein Kinases •
Male • Mitogen-Activated Protein Kinases • Signal
Transduction • cytology • embryology* •
genetics • metabolism • metabolism* • rhoA
GTP-Binding Protein},
Abstract = {The small GTPase Rho is a molecular switch that is best
known for its role in regulating the actomyosin
cytoskeleton. We have investigated its role in the
developing Drosophila embryonic epidermis during the process
of dorsal closure. By expressing the dominant negative
DRhoA(N19) construct in stripes of epidermal cells, we
confirm that Rho function is required for dorsal closure and
demonstrate that it is necessary to maintain the integrity
of the ventral epidermis. We show that defects in actin
organization, nonmuscle myosin II localization, the
regulation of gene transcription, DE-cadherin-based
cell-cell adhesion and cell polarity underlie the effects of
DRhoA(N19) expression. Furthermore, we demonstrate that
these changes in cell physiology have a differential effect
on the epidermis that is dependent upon position in the
dorsoventral axis. In the ventral epidermis, cells either
lose their adhesiveness and fall out of the epidermis or
undergo apoptosis. At the leading edge, cells show altered
adhesive properties such that they form ectopic contacts
with other DRhoA(N19)-expressing cells.},
Key = {fds153500}
}
@article{fds16991,
Author = {Bloor, J.M. and D.P.Kiehart},
Title = {Drosophila RhoA regulates the cytoskeleton and cell-cell
adhesion in the developing epidermis},
Journal = {Development},
Volume = {129},
Pages = {3173-3183},
Year = {2002},
Month = {June},
Key = {fds16991}
}
@article{fds16972,
Author = {T Ohashi and DP Kiehart and HP Erickson},
Title = {Dual labeling of the fibronectin matrix and actin
cytoskeleton with green fluorescent protein
variants.},
Journal = {Journal of cell science, England},
Volume = {115},
Number = {Pt 6},
Pages = {1221-9},
Year = {2002},
Month = {March},
Keywords = {3T3 Cells • Actins • Animals • Cell Movement
• Cells, Cultured • Cytochalasins •
Extracellular Matrix • Fibronectins • Genetic
Vectors • Green Fluorescent Proteins • Indicators
and Reagents • Integrins • Luminescent Proteins
• Mice • Microfilament Proteins •
Microfilaments • Recombinant Fusion Proteins •
analysis • analysis* • chemistry • genetics
• metabolism • pharmacology • physiology
• ultrastructure*},
Abstract = {We have prepared 3T3 cells doubly labeled to visualize
simultaneously the extracellular fibronectin (FN) matrix and
intracellular actin cytoskeleton in living cell cultures. We
used FN-yellow fluorescent protein (FN-yfp) for the FN
matrix, and the actin-binding domain of moesin fused to cyan
fluorescent protein (cfp-Moe) to stain actin. Actin filament
bundles were clearly seen in the protruding lamellae of the
cells. FN matrix assembly appeared to be initiated as small
spots of FN at the ends of actin filament bundles. The spots
then elongated along the actin filament bundle toward the
cell center to form FN fibrils. The end of the fibril
towards the cell edge appeared immobile, and probably
attached to the substrate, whereas the end toward the cell
center frequently showed movements, suggesting attachment to
the cell. Combining our data with the observations of Pankov
et al. we suggest that fibrils grow by stretching this
mobile end toward the cell center while adding new FN
molecules at the end and along the entire length. When the
cell culture was treated with cytochalasin to disrupt the
actin cytoskeleton, some fibrils contracted substantially,
suggesting that the segment attached primarily to the cell
surface is stretched.},
Key = {fds16972}
}
@article{fds16992,
Author = {Dutta, D. and J.W. Bloor and M. Ruiz-Gomez and K. VijayRaghavan and D.P. Kiehart},
Title = {Real-time imaging of morphogenetic movements in Drosophila
using Gal4-UAS-driven expression of GFP fused to the
actin-binding domain of moesin},
Journal = {Genesis},
Volume = {34},
Pages = {146-151},
Year = {2002},
Key = {fds16992}
}
@article{fds16996,
Author = {Kiehart, D.P. and J.D. Franke},
Title = {Actin dynamics: the arp2/3 complex branches
out},
Journal = {Current Biology},
Volume = {12},
Pages = {R557-R559},
Year = {2002},
Key = {fds16996}
}
@article{fds153501,
Author = {JW Bloor and DP Kiehart},
Title = {zipper Nonmuscle myosin-II functions downstream of PS2
integrin in Drosophila myogenesis and is necessary for
myofibril formation.},
Journal = {Developmental biology, United States},
Volume = {239},
Number = {2},
Pages = {215-28},
Year = {2001},
Month = {November},
Keywords = {Actins • Animals • Avian Proteins • Cell
Adhesion • Crosses, Genetic • Cytoplasm •
Drosophila • Drosophila Proteins* • Fibroblasts
• Integrin alpha Chains • Integrins •
Microscopy, Confocal • Microscopy, Fluorescence •
Muscle, Skeletal • Muscles • Mutation •
Myosin Type II • Protein Binding • Protein
Structure, Tertiary • Proteins • Sarcomeres •
Time Factors • Zygote • cytology* •
embryology* • metabolism • metabolism* •
physiology* • rhoA GTP-Binding Protein},
Abstract = {Nonmuscle myosin-II is a key motor protein that drives cell
shape change and cell movement. Here, we analyze the
function of nonmuscle myosin-II during Drosophila embryonic
myogenesis. We find that nonmuscle myosin-II and the
adhesion molecule, PS2 integrin, colocalize at the
developing muscle termini. In the paradigm emerging from
cultured fibroblasts, nonmuscle actomyosin-II contractility,
mediated by the small GTPase Rho, is required to cluster
integrins at focal adhesions. In direct opposition to this
model, we find that neither nonmuscle myosin-II nor RhoA
appear to function in PS2 clustering. Instead, PS2 integrin
is required for the maintenance of nonmuscle myosin-II
localization and we show that the cytoplasmic tail of the
beta(PS) integrin subunit is capable of mediating this PS2
integrin function. We show that embryos that lack zygotic
expression of nonmuscle myosin-II fail to form striated
myofibrils. In keeping with this, we demonstrate that a PS2
mutant that specifically disrupts myofibril formation is
unable to mediate proper localization of nonmuscle myosin-II
at the muscle termini. In contrast, embryos that lack RhoA
function do generate striated muscles. Finally, we find that
nonmuscle myosin-II localizes to the Z-line in mature larval
muscle. We suggest that nonmuscle myosin-II functions at the
muscle termini and the Z-line as an actin crosslinker and
acts to maintain the structural integrity of the
sarcomere.},
Key = {fds153501}
}
@article{fds153502,
Author = {JM Crawford and Z Su and O Varlamova and AR Bresnick and DP
Kiehart},
Title = {Role of myosin-II phosphorylation in V12Cdc42-mediated
disruption of Drosophila cellularization.},
Journal = {European journal of cell biology, Germany},
Volume = {80},
Number = {3},
Pages = {240-4},
Year = {2001},
Month = {March},
Keywords = {Actomyosin • Animals • Binding Sites •
Drosophila • Guanosine Triphosphate • Microscopy,
Fluorescence • Myosins • Phosphorylation •
Protein Binding • Protein-Serine-Threonine Kinases
• Serine • Time Factors • cdc42 GTP-Binding
Protein • chemistry • embryology* •
metabolism • metabolism*},
Abstract = {Microinjection of constitutively active Cdc42 (V12Cdc42)
disrupts the actomyosin cytoskeleton during cellularization
(Crawford et al., Dev. Biol., 204, 151-164 (1998)). The
p21-activated kinase (PAK) family of Ser/Thr kinases are
effectors of GTP-bound forms of the small GTPases, Cdc42 and
Rac. Drosophila PAK, which colocalizes with actin and
myosin-II during cellularization, concentrates at sites of
V12Cdc42-induced actomyosin disruption. In vitro biochemical
analyses demonstrate that PAK phosphorylates the regulatory
light chain (RLC) of Drosophila nonmuscle myosin-II on
Ser21, a site known to activate myosin-II function. Although
activated PAK does not disrupt the actomyosin cytoskeleton,
it induces increased levels of Ser21 phosphorylated RLC.
These findings suggest that increased levels of RLC
phosphorylation do not contribute to disruption of the
actomyosin hexagonal array.},
Key = {fds153502}
}
@article{fds153503,
Author = {Z Su and DP Kiehart},
Title = {Protein kinase C phosphorylates nonmuscle myosin-II heavy
chain from Drosophila but regulation of myosin function by
this enzyme is not required for viability in
flies.},
Journal = {Biochemistry, United States},
Volume = {40},
Number = {12},
Pages = {3606-14},
Year = {2001},
Month = {March},
Keywords = {Amino Acid Sequence • Animals • Avian Proteins
• Drosophila melanogaster • Molecular Sequence
Data • Mutagenesis, Site-Directed • Myosin Heavy
Chains • Myosins • Peptide Fragments •
Phosphorylation • Protein Kinase C • Protein
Structure, Secondary • Proteins • Rabbits •
Rats • Serine • antagonists & inhibitors •
chemistry • enzymology* • genetics • growth &
development* • isolation & purification •
metabolism • metabolism* • physiology*},
Abstract = {Conventional myosins (myosin-IIs) generate forces for cell
shape change and cell motility. Myosin heavy chain
phosphorylation regulates myosin function in simple
eukaryotes and may also be important in metazoans. To
investigate this regulation in a complex eukaryote, we
purified the Drosophila myosin-II tail expressed in
Escherichia coli and showed that it was phosphorylated in
vitro by protein kinase C(PKC) at serines 1936 and 1944,
which are located in the nonhelical globular tail piece.
These sites are close to a conserved serine that is
phosphorylated in vertebrate, nonmuscle myosin-IIs. If the
two serines are mutagenized to alanine or aspartic acid,
phosphorylation no longer occurs. Using a 341 amino acid
tail fragment, we show that there is no difference in the
salt-dependent assembly of wild-type phosphorylated and
mutagenized polypeptides. Thus, the nonmuscle myosin heavy
chain in Drosophila, which is encoded by the zipper gene,
appears to be similar to rabbit nonmuscle myosin-IIA. In
vivo, we generated transgenic flies that expressed the
various myosin heavy chain variants in a zipper null or
near-null genetic background. Like their wild-type
counterparts, such variants are able to completely rescue
the lethal phenotype due to severe zipper mutations. These
results suggest that while the myosin-II heavy chain can be
phosphorylated by PKC, regulation by this enzyme is not
required for viability in Drosophila. Conservation during
530-1000 million years of evolution suggests that regulation
by heavy chain phosphorylation may contribute to nonmuscle
myosin-II function in some real, but minor,
way.},
Key = {fds153503}
}
@article{fds16978,
Author = {Bloor, J.W. and D.P. Kiehart},
Title = {zipper nonmuscle myosin-II functions downstream of PS2
integrin in Drosophila myogenesis and is necessary for
myofibril formation},
Journal = {Dev. Biol.},
Volume = {239},
Pages = {215-228},
Year = {2001},
Key = {fds16978}
}
@article{fds16980,
Author = {Su, Z. and D.P. Kiehart},
Title = {Protein kinase C phosphorylates nonmuscle myosin-II from
Drosophila but regulation of myosin function by this enzyme
is not required for viability in flies},
Journal = {Biochem},
Volume = {40},
Pages = {3606-3614},
Year = {2001},
Key = {fds16980}
}
@article{fds16982,
Author = {Crawford, J.M. and Z. Su and O. Varlamova and A.R. Bresnick and D.P.
Kiehart},
Title = {Role of myosin-II phosphorylation in V12Cdc42-mediated
disruption of Drosophila cellularization},
Journal = {Eur. J. Cell Biol.},
Volume = {80},
Pages = {240-244},
Year = {2001},
Key = {fds16982}
}
@article{fds16995,
Author = {D.P. Kiehart},
Title = {With Malice Towards None},
Journal = {Raleigh News and Observer},
Year = {2001},
Key = {fds16995}
}
@article{fds153504,
Author = {SR Halsell and BI Chu and DP Kiehart},
Title = {Genetic analysis demonstrates a direct link between rho
signaling and nonmuscle myosin function during drosophila
morphogenesis},
Journal = {Genetics, UNITED STATES},
Volume = {156},
Number = {1},
Pages = {469},
Year = {2000},
Month = {September},
Key = {fds153504}
}
@article{fds153505,
Author = {MB Champagne and KA Edwards and HP Erickson and DP
Kiehart},
Title = {Drosophila stretchin-MLCK is a novel member of the
Titin/Myosin light chain kinase family.},
Journal = {Journal of molecular biology, ENGLAND},
Volume = {300},
Number = {4},
Pages = {759-77},
Year = {2000},
Month = {July},
Keywords = {Alternative Splicing • Amino Acid Motifs • Amino
Acid Sequence • Animals • Base Sequence •
Caenorhabditis elegans Proteins* • Catalytic Domain
• Cloning, Molecular • Drosophila Proteins* •
Drosophila melanogaster • Exons • Genes, Insect
• Helminth Proteins • Immunoglobulins •
Insect Proteins • Isoenzymes • Molecular Sequence
Data • Molecular Weight • Multigene Family •
Muscle Proteins • Myosin-Light-Chain Kinase •
Phylogeny • Poly A • Promoter Regions, Genetic
• Protein Kinases • Protein Structure, Tertiary
• RNA, Messenger • Repetitive Sequences, Amino
Acid • Sequence Alignment • analysis •
chemistry • enzymology* • genetics •
genetics* • metabolism • metabolism*},
Abstract = {Members of the titin/myosin light chain kinase family play
an essential role in the organization of the actin/myosin
cytoskeleton, especially in sarcomere assembly and function.
In Drosophila melanogaster, projectin is so far the only
member of this family for which a transcription unit has
been characterized. The locus of another member of this
family, a protein related to Myosin light chain kinase, was
also identified. The cDNA and genomic sequences published
explain only the shorter transcripts expressed by this
locus. Here, we report the complete molecular
characterization of this transcription unit, which spans 38
kb, includes 33 exons and accounts for transcripts up to 25
kb in length. This transcription unit contains both the
largest exon (12,005 nt) and the largest coding region
(25,213 nt) reported so far for Drosophila. This
transcription unit features both internal promoters and
internal polyadenylation signals, which enable it to express
seven different transcripts, ranging from 3.3 to 25 kb in
size. The latter encodes a huge, titin-like, 926 kDa kinase
that features two large PEVK-rich repeats, 32 immunoglobulin
and two fibronectin type-III domains, which we designate
stretchin-MLCK. In addition, the 3' end of the
stretchin-MLCK transcription unit expresses shorter
transcripts that encode 86 to 165 kDa isoforms of
stretchin-MLCK that are analogous to vertebrate Myosin light
chain kinases. Similarly, the 5' end of the Stretchin-Mlck
transcription unit can also express transcripts encoding
kettin and Unc-89-like isoforms, which share no sequences
with the MLCK-like transcripts. Thus, this locus can be
viewed as a single transcription unit, Stretchin-Mlck
(genetic abbreviation Strn-Mlck), that expresses large,
composite transcripts and protein isoforms (sequences
available at http://www.academicpress.com/jmb), as well as a
complex of two independent transcription units, the
Stretchin and Mlck transcription units (Strn and Mlck,
respectively) the result of a "gene fission" event, that
encode independent transcripts and proteins with distinct
structural and enzymatic functions.},
Key = {fds153505}
}
@article{fds153506,
Author = {SR Halsell and BI Chu and DP Kiehart},
Title = {Genetic analysis demonstrates a direct link between rho
signaling and nonmuscle myosin function during Drosophila
morphogenesis.},
Journal = {Genetics, UNITED STATES},
Volume = {155},
Number = {3},
Pages = {1253-65},
Year = {2000},
Month = {July},
Keywords = {Alleles • Animals • Chromosomes • Drosophila
Proteins • Drosophila melanogaster • Genetic
Complementation Test • Guanine Nucleotide Exchange
Factors • Immunoblotting • Membrane Proteins
• Morphogenesis • Mutation, Missense • Myosin
Heavy Chains • Myosins • Physical Chromosome
Mapping • Protein Structure, Tertiary • Signal
Transduction • embryology* • genetics •
genetics* • metabolism • metabolism* • rhoA
GTP-Binding Protein},
Abstract = {A dynamic actomyosin cytoskeleton drives many morphogenetic
events. Conventional nonmuscle myosin-II (myosin) is a key
chemomechanical motor that drives contraction of the actin
cytoskeleton. We have explored the regulation of myosin
activity by performing genetic screens to identify gene
products that collaborate with myosin during Drosophila
morphogenesis. Specifically, we screened for second-site
noncomplementors of a mutation in the zipper gene that
encodes the nonmuscle myosin-II heavy chain. We determined
that a single missense mutation in the zipper(Ebr) allele
gives rise to its sensitivity to second-site
noncomplementation. We then identify the Rho signal
transduction pathway as necessary for proper myosin
function. First we show that a lethal P-element insertion
interacts genetically with zipper. Subsequently we show that
this second-site noncomplementing mutation disrupts the
RhoGEF2 locus. Next, we show that two EMS-induced mutations,
previously shown to interact genetically with zipper(Ebr),
disrupt the RhoA locus. Further, we have identified their
molecular lesions and determined that disruption of the
carboxyl-terminal CaaX box gives rise to their mutant
phenotype. Finally, we show that RhoA mutations themselves
can be utilized in genetic screens. Biochemical and cell
culture analyses suggest that Rho signal transduction
regulates the activity of myosin. Our studies provide direct
genetic proof of the biological relevance of regulation of
myosin by Rho signal transduction in an intact
metazoan.},
Key = {fds153506}
}
@article{fds16986,
Author = {D.P. Kiehart and C.G Galbraith and K.A. Edwards and W.L. Rickoll and R.A. Montague},
Title = {Multiple forces contribute to cell sheet morphogenesis for
dorsal closure in Drosophila},
Journal = {J. Cell Biol.},
Volume = {149},
Pages = {471-490},
Year = {2000},
Month = {April},
Key = {fds16986}
}
@article{fds153507,
Author = {DP Kiehart and CG Galbraith and KA Edwards and WL Rickoll and RA
Montague},
Title = {Multiple forces contribute to cell sheet morphogenesis for
dorsal closure in Drosophila.},
Journal = {The Journal of cell biology, UNITED STATES},
Volume = {149},
Number = {2},
Pages = {471-90},
Year = {2000},
Month = {April},
Keywords = {Animals • Body Patterning • Cell Size •
Drosophila • Embryo, Nonmammalian • Epidermis
• Image Processing, Computer-Assisted • Lasers
• Microscopy, Confocal • Microscopy, Video •
Morphogenesis • Ultraviolet Rays • Wounds and
Injuries • cytology • embryology •
embryology* • physiology* • radiation
effects},
Abstract = {The molecular and cellular bases of cell shape change and
movement during morphogenesis and wound healing are of
intense interest and are only beginning to be understood.
Here, we investigate the forces responsible for
morphogenesis during dorsal closure with three approaches.
First, we use real-time and time-lapsed laser confocal
microscopy to follow actin dynamics and document cell shape
changes and tissue movements in living, unperturbed embryos.
We label cells with a ubiquitously expressed transgene that
encodes GFP fused to an autonomously folding actin binding
fragment from fly moesin. Second, we use a biomechanical
approach to examine the distribution of stiffness/tension
during dorsal closure by following the response of the
various tissues to cutting by an ultraviolet laser. We
tested our previous model (Young, P.E., A.M. Richman, A.S.
Ketchum, and D.P. Kiehart. 1993. Genes Dev. 7:29-41) that
the leading edge of the lateral epidermis is a contractile
purse-string that provides force for dorsal closure. We show
that this structure is under tension and behaves as a
supracellular purse-string, however, we provide evidence
that it alone cannot account for the forces responsible for
dorsal closure. In addition, we show that there is isotropic
stiffness/tension in the amnioserosa and anisotropic
stiffness/tension in the lateral epidermis. Tension in the
amnioserosa may contribute force for dorsal closure, but
tension in the lateral epidermis opposes it. Third, we
examine the role of various tissues in dorsal closure by
repeated ablation of cells in the amnioserosa and the
leading edge of the lateral epidermis. Our data provide
strong evidence that both tissues appear to contribute to
normal dorsal closure in living embryos, but surprisingly,
neither is absolutely required for dorsal closure. Finally,
we establish that the Drosophila epidermis rapidly and
reproducibly heals from both mechanical and ultraviolet
laser wounds, even those delivered repeatedly. During
healing, actin is rapidly recruited to the margins of the
wound and a newly formed, supracellular purse-string
contracts during wound healing. This result establishes the
Drosophila embryo as an excellent system for the
investigation of wound healing. Moreover, our observations
demonstrate that wound healing in this insect epidermal
system parallel wound healing in vertebrate tissues in situ
and vertebrate cells in culture (for review see Kiehart,
D.P. 1999. Curr. Biol. 9:R602-R605).},
Key = {fds153507}
}
@article{fds16983,
Author = {Halsell, SR, BI Chu and DP Kiehart},
Title = {Genetic analysis demonstrates a direct link between Rho
signaling and nonmuscle myosin function during Drosophila
morphogenesis},
Journal = {Genetics},
Volume = {155},
Pages = {1253-1265},
Year = {2000},
Key = {fds16983}
}
@article{fds16984,
Author = {Champagne, M.B. and K.A. Edwards and H.P. Erickson and D.P.
Kiehart},
Title = {Drosophila stretchin-MLCK is a novel member of the
titn/myosin light chain kinase family},
Journal = {J. Molec. Biol.},
Volume = {300},
Pages = {759-777},
Year = {2000},
Key = {fds16984}
}
@article{fds153508,
Author = {DP Kiehart},
Title = {Wound healing: The power of the purse string.},
Journal = {Current biology : CB, ENGLAND},
Volume = {9},
Number = {16},
Pages = {R602-5},
Year = {1999},
Month = {August},
Keywords = {Actins • Actomyosin • Animals • Drosophila
melanogaster • Embryo, Nonmammalian • Female
• Microscopy, Fluorescence • Myosins •
Oocytes • Ovum • Sea Urchins • Wound Healing
• Xenopus • chemistry • embryology •
physiology • physiology*},
Abstract = {Recently, Xenopus oocytes have been shown to repair wounds
using a contractile system composed of actin and myosin-II.
The work underscores the importance of actin-based myosin-II
contractility in cellular and supracellular 'purse strings'
that function in diverse biological processes.},
Key = {fds153508}
}
@article{fds153509,
Author = {JM Crawford and DP Kiehart},
Title = {Biology in pictures: From one cell to many.},
Journal = {Current biology : CB, ENGLAND},
Volume = {9},
Number = {11},
Pages = {R389},
Year = {1999},
Month = {June},
Keywords = {Animals • Drosophila • embryology* •
genetics*},
Key = {fds153509}
}
@article{fds153510,
Author = {T Ohashi and DP Kiehart and HP Erickson},
Title = {Dynamics and elasticity of the fibronectin matrix in living
cell culture visualized by fibronectin-green fluorescent
protein.},
Journal = {Proceedings of the National Academy of Sciences of the
United States of America, UNITED STATES},
Volume = {96},
Number = {5},
Pages = {2153-8},
Year = {1999},
Month = {March},
Keywords = {Amino Acid Sequence • Animals • CHO Cells •
Cell Membrane • Cells, Cultured • Cricetinae
• Elasticity • Extracellular Matrix •
Fibronectins • Green Fluorescent Proteins •
Kinetics • Luminescent Proteins • Mutagenesis,
Insertional • Polymerase Chain Reaction •
Recombinant Fusion Proteins • Time Factors •
Transfection • analysis • analysis* •
chemistry • genetics • metabolism •
physiology* • ultrastructure},
Abstract = {Fibronectin (FN) forms the primitive fibrillar matrix in
both embryos and healing wounds. To study the matrix in
living cell cultures, we have constructed a cell line that
secretes FN molecules chimeric with green fluorescent
protein. These FN-green fluorescent protein molecules were
assembled into a typical matrix that was easily visualized
by fluorescence over periods of several hours. FN fibrils
remained mostly straight, and they were seen to extend and
contract to accommodate movements of the cells, indicating
that they are elastic. When fibrils were broken or detached
from cells, they contracted to less than one-fourth of their
extended length, demonstrating that they are highly
stretched in the living culture. Previous work from other
laboratories has suggested that cryptic sites for FN
assembly may be exposed by tension on FN. Our results show
directly that FN matrix fibrils are not only under tension
but are also highly stretched. This stretched state of FN is
an obvious candidate for exposing the cryptic assembly
sites.},
Key = {fds153510}
}
@article{fds16959,
Author = {Ohashi, T. and D.P. Kiehart and H.P. Erickson},
Title = {Dynamics and elasticity of the fibronectin matrix in living
cell culture visualized by fibronectin–green fluorescent
protein},
Journal = {Proc. Natl. Acad. Sci. USA},
Volume = {96},
Pages = {2153-2158},
Year = {1999},
Key = {fds16959}
}
@article{fds16993,
Author = {D.P. Kiehart},
Title = {Wound healing: The power of the purse-string},
Journal = {Current Biology},
Volume = {9194935508},
Pages = {R602-R605},
Year = {1999},
Key = {fds16993}
}
@article{fds16994,
Author = {Crawford, J.M. and D.P. Kiehart},
Title = {Biology in pictures: From one cell to many},
Journal = {Current Biology},
Volume = {9},
Pages = {R389},
Year = {1999},
Key = {fds16994}
}
@article{fds153511,
Author = {JM Crawford and N Harden and T Leung and L Lim and DP
Kiehart},
Title = {Cellularization in Drosophila melanogaster is disrupted by
the inhibition of rho activity and the activation of Cdc42
function.},
Journal = {Developmental biology, UNITED STATES},
Volume = {204},
Number = {1},
Pages = {151-64},
Year = {1998},
Month = {December},
Keywords = {Animals • Cell Cycle Proteins • Cell
Differentiation • Cell Division • Cytoskeleton
• Drosophila melanogaster • Embryo, Nonmammalian
• GTP-Binding Proteins • Membrane Proteins •
Signal Transduction • cdc42 GTP-Binding Protein,
Saccharomyces cerevisiae • cytology* • embryology
• physiology • physiology* • rhoB GTP-Binding
Protein},
Abstract = {Regulation of cytoskeletal dynamics is essential for cell
shape change and morphogenesis. Drosophila melanogaster
embryos offer a well-defined system for observing
alterations in the cytoskeleton during the process of
cellularization, a specialized form of cytokinesis. During
cellularization, the actomyosin cytoskeleton forms a
hexagonal array and drives invagination of the plasma
membrane between the nuclei located at the cortex of the
syncytial blastoderm. Rho, Rac, and Cdc42 proteins are
members of the Rho subfamily of Ras-related G proteins that
are involved in the formation and maintenance of the actin
cytoskeleton throughout phylogeny and in D. melanogaster. To
investigate how Rho subfamily activity affects the
cytoskeleton during cellularization stages, embryos were
microinjected with C3 exoenzyme from Clostridium botulinum
or with wild-type, constitutively active, or dominant
negative versions of Rho, Rac, and Cdc42 proteins. C3
exoenzyme ADP-ribosylates and inactivates Rho with high
specificity, whereas constitutively active dominant
mutations remain in the activated GTP-bound state to
activate downstream effectors. Dominant negative mutations
likely inhibit endogenous small G protein activity by
sequestering exchange factors. Of the 10 agents
microinjected, C3 exoenzyme, constitutively active Cdc42,
and dominant negative Rho have a specific and
indistinguishable effect: the actomyosin cytoskeleton is
disrupted, cellularization halts, and embryogenesis arrests.
Time-lapse video records of DIC imaged embryos show that
nuclei in injected regions move away from the cortex of the
embryo, thereby phenocopying injections of cytochalasin or
antimyosin. Rhodamine phalloidin staining reveals that the
actin-based hexagonal array normally seen during
cellularization is disrupted in a dose-dependent fashion.
Additionally, DNA stain reveals that nuclei in the
microinjected embryos aggregate in regions that correspond
to actin disruption. These embryos halt in cellularization
and do not proceed to gastrulation. We conclude that Rho
activity and Cdc42 regulation are required for cytoskeletal
function in actomyosin-driven furrow canal formation and
nuclear positioning.},
Key = {fds153511}
}
@article{fds153512,
Author = {PG Aitken and AJ Borgdorff and AJ Juta and DP Kiehart and GG Somjen and WJ
Wadman},
Title = {Volume changes induced by osmotic stress in freshly isolated
rat hippocampal neurons.},
Journal = {Pflügers Archiv : European journal of physiology,
GERMANY},
Volume = {436},
Number = {6},
Pages = {991-8},
Year = {1998},
Month = {November},
Keywords = {Animals • Cell Membrane Permeability • Cell Size*
• Hippocampus • Hypertonic Solutions •
Hypotonic Solutions* • Kinetics • Mannitol •
Neurons • Osmolar Concentration • Rats •
Sodium Chloride • administration & dosage •
cytology*},
Abstract = {The degree to which osmotic stress changes the volume of
mammalian central neurons has not previously been
determined. We isolated CA1 pyramidal cells and measured
cell volume in four different ways. Extracellular osmolarity
(pio) was lowered by omitting varying amounts of NaCl and
raised by adding mannitol; the extremes of pio tested ranged
from 134 to 396 mosm/kg. When pio was reduced, cell swelling
varied widely. We distinguished three types of cells
according to their response: "yielding cells" whose volume
began to increase immediately; "delayed response cells"
which swelled after a latent period of 2 min or more; and
"resistant cells" whose volume did not change during
exposure to hypo-osmotic solution. When pio was raised, most
cells shrank slowly, reaching minimal volume in 15-20 min.
We observed neither a regulatory volume decrease nor an
increase. We conclude that the water permeability of the
membrane of hippocampal CA1 pyramidal neurons is low
compared to that of other cell types. The mechanical support
of the plasma membrane given by the cytoskeleton may
contribute to the resistance to swelling and protect neurons
against swelling-induced damage.},
Key = {fds153512}
}
@article{fds153513,
Author = {GH Thomas and DC Zarnescu and AE Juedes and MA Bales and A Londergan and CC
Korte, DP Kiehart},
Title = {Drosophila betaHeavy-spectrin is essential for development
and contributes to specific cell fates in the
eye.},
Journal = {Development (Cambridge, England), ENGLAND},
Volume = {125},
Number = {11},
Pages = {2125-34},
Year = {1998},
Month = {June},
Keywords = {Alleles • Animals • Cadherins • Cell Adhesion
• Cell Communication • Drosophila •
Drosophila Proteins* • Eye • Eye Abnormalities
• Gene Expression • Genes, Insect •
Infertility • Insect Proteins • Microvilli •
Mutation • Phenotype • Photoreceptor Cells,
Invertebrate • Spectrin • Wing •
abnormalities • embryology • embryology* •
genetics • genetics* • metabolism*},
Abstract = {The spectrin membrane skeleton is a ubiquitous cytoskeletal
structure with several cellular roles, including the
maintenance of cell integrity, determination of cell shape
and as a contributor to cell polarity. We have isolated
mutations in the gene encoding &bgr ;Heavy-spectrin in
Drosophila, and have named this essential locus karst. karst
mutant individuals have a pleiotropic phenotype
characterized by extensive larval lethality and, in adult
escapers, rough eyes, bent wings, tracheal defects and
infertility. Within karst mutant eyes, a significant number
of ommatidia specifically lack photoreceptor R7 alongside
more complex morphological defects. Immunolocalization of
betaHeavy-spectrin in wild-type eye-antennal and wing
imaginal discs reveals that betaHeavy-spectrin is present in
a restricted subdomain of the membrane skeleton that
colocalizes with DE-cadherin. We propose a model where
normal levels of Sevenless signaling are dependent on tight
cell-cell adhesion facilitated by the betaHeavy-spectrin
membrane skeleton. Immunolocalization of betaHeavy-spectrin
in the adult and larval midgut indicates that it is a
terminal web protein, but we see no gross morphological
defects in the adult apical brush border in karst mutant
flies. Rhodamine phalloidin staining of karst mutant ovaries
similarly reveals no conspicuous defect in the actin
cytoskeleton or cellular morphology in egg chambers. This is
in contrast to mutations in alpha-spectrin, the molecular
partner of betaHeavy-spectrin, which affect cellular
structure in both the larval gut and adult ovaries. Our
results emphasize the fundamental contribution of the
spectrin membrane skeleton to normal development and reveals
a critical interplay between the integrity of a cell's
membrane skeleton, the structure of cell-cell contacts and
cell signaling.},
Key = {fds153513}
}
@article{fds153514,
Author = {SR Halsell and DP Kiehart},
Title = {Second-site noncomplementation identifies genomic regions
required for Drosophila nonmuscle myosin function during
morphogenesis.},
Journal = {Genetics, UNITED STATES},
Volume = {148},
Number = {4},
Pages = {1845-63},
Year = {1998},
Month = {April},
Keywords = {Animals • Binding Sites • Chromosome Aberrations
• Drosophila • Drosophila Proteins • Genetic
Complementation Test • Membrane Proteins •
Morphogenesis* • Myosin Heavy Chains • X
Chromosome • genetics* • growth & development
• physiology*},
Abstract = {Drosophila is an ideal metazoan model system for analyzing
the role of nonmuscle myosin-II (henceforth, myosin) during
development. In Drosophila, myosin function is required for
cytokinesis and morphogenesis driven by cell migration
and/or cell shape changes during oogenesis, embryogenesis,
larval development and pupal metamorphosis. The mechanisms
that regulate myosin function and the supramolecular
structures into which myosin incorporates have not been
systematically characterized. The genetic screens described
here identify genomic regions that uncover loci that
facilitate myosin function. The nonmuscle myosin heavy chain
is encoded by a single locus, zipper. Contiguous chromosomal
deficiencies that represent approximately 70% of the
euchromatic genome were screened for genetic interactions
with two recessive lethal alleles of zipper in a second-site
noncomplementation assay for the malformed phenotype.
Malformation in the adult leg reflects aberrations in cell
shape changes driven by myosin-based contraction during leg
morphogenesis. Of the 158 deficiencies tested, 47 behaved as
second-site noncomplementors of zipper. Two of the
deficiencies are strong interactors, 17 are intermediate and
28 are weak. Finer genetic mapping reveals that mutations in
cytoplasmic tropomyosin and viking (collagen IV) behave as
second-site noncomplementors of zipper during leg
morphogenesis and that zipper function requires a previously
uncharacterized locus, E3.10/J3.8, for leg morphogenesis and
viability.},
Key = {fds153514}
}
@article{fds153515,
Author = {GH Thomas and EC Newbern and CC Korte and MA Bales and SV Muse and AG
Clark, DP Kiehart},
Title = {Intragenic duplication and divergence in the spectrin
superfamily of proteins.},
Journal = {Molecular biology and evolution, UNITED STATES},
Volume = {14},
Number = {12},
Pages = {1285-95},
Year = {1997},
Month = {December},
Keywords = {Actinin • Amino Acid Sequence • Animals •
Dystrophin • Evolution, Molecular* • Humans •
Models, Genetic • Molecular Sequence Data •
Protein Precursors • Repetitive Sequences, Nucleic
Acid* • Sequence Homology, Amino Acid • Spectrin
• chemistry • genetics • genetics*},
Abstract = {Many structural, signaling, and adhesion molecules contain
tandemly repeated amino acid motifs. The
alpha-actinin/spectrin/dystrophin superfamily of
F-actin-crosslinking proteins contains an array of triple
alpha-helical motifs (spectrin repeats). We present here the
complete sequence of the novel beta-spectrin isoform
beta(Heavy)-spectrin (beta H). The sequence of beta H
supports the origin of alpha- and beta-spectrins from a
common ancestor, and we present a novel model for the origin
of the spectrins from a homodimeric actin-crosslinking
precursor. The pattern of similarity between the spectrin
repeat units indicates that they have evolved by a series of
nested, nonuniform duplications. Furthermore, the spectrins
and dystrophins clearly have common ancestry, yet the repeat
unit is of a different length in each family. Together,
these observations suggest a dynamic period of increase in
repeat number accompanied by homogenization within each
array by concerted evolution. However, today, there is
greater similarity of homologous repeats between species
than there is across repeats within species, suggesting that
concerted evolution ceased some time before the
arthropod/vertebrate split. We propose a two-phase model for
the evolution of the spectrin repeat arrays in which an
initial phase of concerted evolution is subsequently
retarded as each new protein becomes constrained to a
specific length and the repeats diverge at the DNA level.
This evolutionary model has general applicability to the
origins of the many other proteins that have tandemly
repeated motifs.},
Key = {fds153515}
}
@article{fds153516,
Author = {KA Edwards and M Demsky and RA Montague and N Weymouth and DP
Kiehart},
Title = {GFP-moesin illuminates actin cytoskeleton dynamics in living
tissue and demonstrates cell shape changes during
morphogenesis in Drosophila.},
Journal = {Developmental biology, UNITED STATES},
Volume = {191},
Number = {1},
Pages = {103-17},
Year = {1997},
Month = {November},
Keywords = {Amino Acid Sequence • Animals • Animals,
Genetically Modified • Drosophila • Embryo,
Nonmammalian • Female • Gene Expression
Regulation, Developmental • Green Fluorescent Proteins
• HSP70 Heat-Shock Proteins • Luminescent Proteins
• Microfilament Proteins* • Morphogenesis •
Nervous System • Neurons • Ovary • Promoter
Regions, Genetic • Protein Biosynthesis* •
Proteins • Pupa • Recombinant Fusion Proteins
• Scyphozoa • biosynthesis • chemistry •
cytology • embryology • embryology* •
genetics • physiology • physiology*},
Abstract = {Moesin, ezrin, and radixin (MER) are components of the
cortical actin cytoskeleton and membrane processes such as
filopodia and microvilli. Their C-terminal tails contain an
extended region that is predicted to be helical, an actin
binding domain, and a region(s) that participates in
self-association. We engineered an in vivo fluorescent actin
binding protein (GFP-moe) by joining sequences that encode
the jellyfish green fluorescent protein (GFP) to sequences
that encode the C-terminal end of the sole Drosophila MER
homolog, moesin [Moesin-like gene product, referred to
previously as the D17 MER-like protein; Edwards et al.,
1994, Proc. Natl. Acad. Sci. USA 91, 4589], and Dmoesin
[McCartney and Fehon, 1996, J. Cell Biol. 133, 843].
Transgenic flies expressing this fusion protein under
control of the hsp70 promoter were generated and used for
analysis of cell shape changes during morphogenesis of
various developmental stages and tissues. Following heat
shock, high levels of stable fusion protein are produced by
all somatic tissues. GFP-moe localizes to the cortical actin
cytoskeleton, providing a strong in vivo marker for cell
shape and pattern during epithelial morphogenesis. The
protein also becomes highly enriched in pseudopods,
microvilli, axons, denticles, the border cell process, and
other membrane projections, potentially by binding to
endogenous moesin as well as actin. We show that GFP-moe can
be used to examine the development and behavior of these
dynamic structures in live specimens. We observe a bright
green fluorescent, presumably actin-rich, polar cell
proboscis that inserts itself into the forming micropyle and
appears to maintain an opening for sperm passage around
which the chorion is formed. We also confirm the existence
of an actin-rich purse string at the leading edge of the
lateral epidermis and provide a dynamic analysis of its
behavior as it migrates during dorsal closure. Observations
of embryos, larvae, and pupae show that GFP-moe is also
useful for labeling the developing nervous system and will
be a good general marker of dynamic cell behavior during
morphogenesis in live tissues and demonstrate that fusion of
a subcellular localization signal to GFP greatly increases
its utility as a cell marker.},
Key = {fds153516}
}
@article{fds153517,
Author = {JD Pederson and DP Kiehart and JW Mahaffey},
Title = {The role of HOM-C genes in segmental transformations:
reexamination of the Drosophila Sex combs reduced embryonic
phenotype.},
Journal = {Developmental biology, UNITED STATES},
Volume = {180},
Number = {1},
Pages = {131-42},
Year = {1996},
Month = {November},
Keywords = {Animals • Drosophila Proteins* • Drosophila
melanogaster • Embryo, Nonmammalian • Gene
Expression Regulation, Developmental* • Genes,
Homeobox* • Genes, Insect* • Homeodomain Proteins
• In Situ Hybridization • Insect Hormones •
Mutagenesis • Phenotype • Transcription Factors*
• Transcription, Genetic • biosynthesis* •
embryology* • genetics • genetics* •
physiology},
Abstract = {Homeotic genes in the Antennapedia Complex of Drosophila
specify identity of the posterior head segments; the labial
segment requires Sex combs reduced (Scr) for proper
development, Deformed (Dfd) specifies maxillary and
mandibular identity, and labial is necessary for intercalary
segment identity. Although mutations in these genes cause
homeotic transformations during imago development, the only
obvious homeotic transformation during embryonic head
development is found in Scr mutants, where a partial
transformation of the labial segment to a more anterior,
maxillary identity has been reported. This transformation is
unusual because DFD protein does not accumulate in the
labial cells of Scr mutants, although DFD is required for
development of maxillary structures. Here, we present
evidence that casts doubt on whether the labial to maxillary
transformation actually exists in embryos lacking Scr. The
observed morphological characteristics and gene expression
patterns of various mutant embryos indicate a loss of
segmental identity rather than a transformation.},
Key = {fds153517}
}
@article{fds153518,
Author = {JA Cooper and DP Kiehart},
Title = {Septins may form a ubiquitous family of cytoskeletal
filaments.},
Journal = {The Journal of cell biology, UNITED STATES},
Volume = {134},
Number = {6},
Pages = {1345-8},
Year = {1996},
Month = {September},
Keywords = {Cell Cycle Proteins • Cytoskeletal Proteins* •
Cytoskeleton • Fungal Proteins • GTP
Phosphohydrolases • Membrane Proteins •
Saccharomyces cerevisiae Proteins* •
Schizosaccharomyces pombe Proteins • Transcription
Factors • chemistry* • physiology •
physiology*},
Key = {fds153518}
}
@article{fds153519,
Author = {KA Edwards and DP Kiehart},
Title = {Drosophila nonmuscle myosin II has multiple essential roles
in imaginal disc and egg chamber morphogenesis.},
Journal = {Development (Cambridge, England), ENGLAND},
Volume = {122},
Number = {5},
Pages = {1499-511},
Year = {1996},
Month = {May},
Keywords = {Actomyosin • Animals • Cell Movement •
Dictyostelium • Drosophila • Extremities •
Female • Fluorescent Antibody Technique • Gene
Expression Regulation, Developmental • Genes, Lethal
• Heat-Shock Response • Morphogenesis •
Myosins • Oogenesis* • Photoreceptor Cells,
Invertebrate • Species Specificity • Time Factors
• Tissue Distribution • embryology •
embryology* • genetics • growth & development
• isolation & purification • physiology •
physiology*},
Abstract = {Morphogenesis is characterized by orchestrated changes in
the shape and position of individual cells. Many of these
movements are thought to be powered by motor proteins.
However, in metazoans, it is often difficult to match
specific motors with the movements they drive. The nonmuscle
myosin II heavy chain (MHC encoded by zipper is required for
cell sheet movements in Drosophila embryos. To determine if
myosin II is required for other processes, we examined the
phenotypes of strong and weak larval lethal mutations in
spaghetti squash (sqh), which encodes the nonmuscle myosin
II regulatory light chain (RLC). sqh mutants can be rescued
to adulthood by daily induction of a sqh cDNA transgene
driven by the hsp70 promoter. By transiently ceasing
induction of the cDNA, we depleted RLC at specific times
during development. When RLC is transiently depleted in
larvae, the resulting adult phenotypes demonstrate that RLC
is required in a stage-specific fashion for proper
development of eye and leg imaginal discs. When RLC is
depleted in adult females, oogenesis is reversibly
disrupted. Without RLC induction, developing egg chambers
display a succession of phenotypes that demonstrate roles
for myosin II in morphogenesis of the interfollicular
stalks, three morphologically and mechanistically distinct
types of follicle cell migration, and completion of nurse
cell cytoplasm transport (dumping). Finally, we show that in
sqh mutant tissues, MHC is abnormally localized in punctate
structures that do not contain appreciable amounts of
filamentous actin or the myosin tail-binding protein p127.
This suggests that sqh mutant phenotypes are chiefly caused
by sequestration of myosin into inactive aggregates. These
results show that myosin II is responsible for a
surprisingly diverse array of cell shape changes throughout
development.},
Key = {fds153519}
}
@article{fds153520,
Author = {SG Mansfield and DY al-Shirawi, AS Ketchum and EC Newbern and DP
Kiehart},
Title = {Molecular organization and alternative splicing in zipper,
the gene that encodes the Drosophila non-muscle myosin II
heavy chain.},
Journal = {Journal of molecular biology, ENGLAND},
Volume = {255},
Number = {1},
Pages = {98-109},
Year = {1996},
Month = {January},
Keywords = {Alleles • Alternative Splicing • Amino Acid
Sequence • Animals • Base Sequence • DNA
Mutational Analysis • Drosophila Proteins •
Drosophila melanogaster • Genes, Insect • Membrane
Proteins • Molecular Sequence Data • Myosin Heavy
Chains • Protein Structure, Secondary • RNA,
Messenger • Regulatory Sequences, Nucleic Acid •
Sequence Alignment • chemistry • genetics •
genetics*},
Abstract = {Genomic sequence of the entire zipper gene, that encodes
non-muscle myosin II heavy chain (MHC) in Drosophila
melanogaster, reveals a new, differentially spliced exon in
this essential locus and identifies a molecular lesion that
is responsible for a severe embryonic lethal zipper allele.
There are two alternative splices in the head domain. The
first is present in the 5' untranslated sequence which, when
employed, produces an N-terminal extension of 45 amino acids
(aa). This splicoform produces a protein that is stable in
flies but less prevalent than the isoform that lacks the
extension. The second alternative exon (40 aa) is close to
the nucleotide binding pocket. The position, size and
sequence of this exon is conserved in D. simulans and
putative alternative exons of different size (7 to 16 aa)
but identical position have been reported for other myosins
throughout phylogeny. The functional significance of neither
alternative splice is clear. Sequence analysis of genomic
DNA identifies the lesion responsible for zipIIF107, one of
the original severe embryonic lethal zipper alleles. Our
primary structural data confirm and correct our previous
sequence of the cDNA, establish the spatial relationship
between zipper and unzipped (the gene originally thought to
have been disrupted in zipper mutations), and provide a high
resolution template for the precise mapping of
mutations.},
Key = {fds153520}
}
@article{fds153521,
Author = {KA Edwards and XJ Chang and DP Kiehart},
Title = {Essential light chain of Drosophila nonmuscle myosin
II.},
Journal = {Journal of muscle research and cell motility,
ENGLAND},
Volume = {16},
Number = {5},
Pages = {491-8},
Year = {1995},
Month = {October},
Keywords = {Animals • Base Sequence • Chromosome Mapping
• Chromosomes • Cloning, Molecular • DNA,
Complementary • Drosophila melanogaster •
Molecular Sequence Data • Myosin Light Chains •
Myosins • Polymerase Chain Reaction • Protein
Structure, Tertiary • Sequence Analysis, DNA •
Sequence Homology, Amino Acid • chemistry •
genetics • genetics* • ultrastructure},
Abstract = {We have cloned and sequenced a cDNA encoding the essential
(alkaline) light chain of nonmuscle myosin from Drosophila
melanogaster. The protein predicted from the cDNA matches
partial amino acid sequence derived from essential light
chain protein that copurifies with native nonmuscle myosin
heavy chain. This completes the sequence of the three myosin
subunits, two of which have been shown genetically to be
required for morphogenesis and cytokinesis (the heavy chain
encoded by zipper and the regulatory light chain encoded by
spaghetti squash). The essential light chain protein is 147
amino acids in length and is 53% identical to human smooth
muscle essential light chain. The sequence is consistent
with the presence of four helix-loop-helix domains seen in
crystallographic structures of the striated muscle myosin
light chains and their close relative, calmodulin. We
identified the most conserved residues among essential light
chain sequences from multiple phyla and present their
locations on the crystallographic structure of striated
muscle essential light chain. This highlights several
conserved contacts among the myosin subunits that may be
important for the structure and regulation of the myosin
motor. The gene encoding Drosophila nonmuscle essential
light chain (Mlc-c) localizes to cytological position 5A6
and we discuss prospects for genetic analysis in this
region.},
Key = {fds153521}
}
@article{fds153522,
Author = {KG Miller and DP Kiehart},
Title = {Fly division.},
Journal = {The Journal of cell biology, UNITED STATES},
Volume = {131},
Number = {1},
Pages = {1-5},
Year = {1995},
Month = {October},
Keywords = {Animals • Cell Division • Drosophila •
cytology* • physiology},
Key = {fds153522}
}
@article{fds153523,
Author = {GH Thomas and DP Kiehart},
Title = {Beta heavy-spectrin has a restricted tissue and subcellular
distribution during Drosophila embryogenesis.},
Journal = {Development (Cambridge, England), ENGLAND},
Volume = {120},
Number = {7},
Pages = {2039-50},
Year = {1994},
Month = {July},
Keywords = {Animals • Cell Membrane • Drosophila •
Embryo, Nonmammalian • Fluorescent Antibody Technique
• Gastrula • Immunoblotting • In Situ
Hybridization • Morphogenesis • Ovum •
Spectrin • analysis* • chemistry* •
embryology* • physiology},
Abstract = {The components of the membrane skeleton play an important
role in maintaining membrane structure during the dynamic
changes in cell shape that characterize development. beta
Heavy-spectrin is a unique beta-spectrin from Drosophila
melanogaster that is closer in size (M(r) = 430 x 10(3)) to
dystrophin than to other beta-spectrin members of the
spectrin/alpha-actinin/dystrophin gene super-family. Here we
establish that both the subcellular localization of the beta
Heavy-spectrin protein and the tissue distribution of beta
Heavy-spectrin transcript accumulation change dramatically
during embryonic development. Maternally loaded protein is
uniformly distributed around the plasma membrane of the egg.
During cellularization it is associated with the
invaginating furrow canals and in a region of the lateral
membranes at the apices of the forming cells (apicolateral).
During gastrulation the apicolateral staining remains and is
joined by a new apical cap, or plate, of beta Heavy-spectrin
in areas where morphogenetic movements occur. These
locations include the ventral and cephalic furrows and the
posterior midgut invagination. Thus, dynamic rearrangement
of the subcellular distribution of the protein is precisely
coordinated with changes in cell shape. Zygotic message and
protein accumulate after the germ band is fully extended, in
the musculature, epidermis, hindgut, and trachea of the
developing embryo. beta Heavy-spectrin in the epidermis,
hindgut, and trachea is apically localized, while the
protein in the somatic and visceral musculature is not
obviously polarized. The distribution of beta Heavy-spectrin
suggests roles in establishing an apicolateral membrane
domain that is known to be rich in intercellular junctions
and in establishing a unique membrane domain associated with
contractile processes.},
Key = {fds153523}
}
@article{fds153524,
Author = {KA Edwards and RA Montague and S Shepard and BA Edgar and RL Erikson and DP
Kiehart},
Title = {Identification of Drosophila cytoskeletal proteins by
induction of abnormal cell shape in fission
yeast.},
Journal = {Proceedings of the National Academy of Sciences of the
United States of America, UNITED STATES},
Volume = {91},
Number = {10},
Pages = {4589-93},
Year = {1994},
Month = {May},
Keywords = {Actin Depolymerizing Factors • Amino Acid Sequence
• Animals • Cloning, Molecular • Conserved
Sequence • Cytoskeletal Proteins • Drosophila
melanogaster • Gene Library • Genetic Vectors
• Humans • Microfilament Proteins • Molecular
Sequence Data • Nerve Tissue Proteins •
Schizosaccharomyces • Sequence Homology, Amino Acid
• Vertebrates • biosynthesis • biosynthesis*
• genetics • methods* • physiology •
physiology*},
Abstract = {To clone metazoan genes encoding regulators of cell shape,
we have developed a functional assay for proteins that
affect the morphology of a simple organism, the fission
yeast Schizosaccharomyces pombe. A Drosophila melanogaster
cDNA library was constructed in an inducible expression
vector and transformed into S. pombe. When expression of the
Drosophila sequences was induced, aberrant cell shapes were
found in 0.2% of the transformed colonies. Four severe
phenotypes representing defects in cytokinesis and/or cell
shape maintenance were examined further. Each displayed
drastic and specific reorganizations of the actin
cytoskeleton. Three of the cDNAs responsible for these
defects appear to encode cytoskeletal components: the actin
binding proteins profilin and cofilin/actin depolymerizing
factor and a membrane-cytoskeleton linker of the
ezrin/merlin family. These results demonstrate that a yeast
phenotypic screen efficiently identifies conserved genes
from more complex organisms and sheds light on their
potential in vivo functions.},
Key = {fds153524}
}
@article{fds153525,
Author = {DP Kiehart and RA Montague and WL Rickoll and D Foard and GH
Thomas},
Title = {High-resolution microscopic methods for the analysis of
cellular movements in Drosophila embryos.},
Journal = {Methods in cell biology, UNITED STATES},
Volume = {44},
Pages = {507-32},
Year = {1994},
Keywords = {Animals • Cell Movement • Drosophila melanogaster
• Embryo, Nonmammalian • Image Processing,
Computer-Assisted • Microscopy • cytology •
cytology* • embryology* • methods* •
physiology},
Key = {fds153525}
}
@article{fds153526,
Author = {PE Young and AM Richman and AS Ketchum and DP Kiehart},
Title = {Morphogenesis in Drosophila requires nonmuscle myosin heavy
chain function.},
Journal = {Genes & development, UNITED STATES},
Volume = {7},
Number = {1},
Pages = {29-41},
Year = {1993},
Month = {January},
Keywords = {Animals • Base Sequence • DNA • Drosophila
• Female • Genetic Complementation Test •
Immunoblotting • Male • Molecular Sequence Data
• Morphogenesis • Muscles • Mutation •
Myosins • embryology • embryology* • genetics
• metabolism • physiology*},
Abstract = {We provide the first link between a known molecular motor
and morphogenesis, the fundamental process of cell shape
changes and movements that characterizes development
throughout phylogeny. By reverse genetics, we generate
mutations in the Drosophila conventional nonmuscle myosin
(myosin II) heavy chain gene and show that this gene is
essential. We demonstrate that these mutations are allelic
to previously identified, recessive, embryonic-lethal zipper
mutations and thereby identify nonmuscle myosin heavy chain
as the zipper gene product. Embryos that lack functional
myosin display defects in dorsal closure, head involution,
and axon patterning. Analysis of cell morphology and myosin
localization during dorsal closure in wild-type and
homozygous mutant embryos demonstrates a key role for myosin
in the maintenance of cell shape and suggests a model for
the involvement of myosin in cell sheet movement during
development. Our experiments, in conjunction with the
observation that cytokinesis also requires myosin, suggest
that the processes of cell shape change in morphogenesis and
cell division are intimately and mechanistically
related.},
Key = {fds153526}
}
@article{fds153527,
Author = {RE Karess and XJ Chang and KA Edwards and S Kulkarni and I Aguilera and DP
Kiehart},
Title = {The regulatory light chain of nonmuscle myosin is encoded by
spaghetti-squash, a gene required for cytokinesis in
Drosophila.},
Journal = {Cell, UNITED STATES},
Volume = {65},
Number = {7},
Pages = {1177-89},
Year = {1991},
Month = {June},
Keywords = {Alleles • Amino Acid Sequence • Animals •
Base Sequence • Blotting, Northern • Blotting,
Southern • Cell Division* • Chromosome Mapping
• Cloning, Molecular • Drosophila melanogaster
• Gene Expression • Genes • Mitosis •
Molecular Sequence Data • Mutation • Myosins
• Nucleic Acid Hybridization • Phenotype •
RNA, Messenger • Restriction Mapping •
Transcription, Genetic • genetics • genetics*
• physiology},
Abstract = {Two independent approaches to understanding the molecular
mechanism of cytokinesis have converged on the gene
spaghetti-squash (sqh). A genetic screen for mitotic mutants
identified sqh1, a mutation that disrupts cytokinesis, which
was then cloned by transposon tagging. Independently, the
gene that encodes the regulatory light chain of the
biochemically defined nonmuscle myosin (MRLC-C) was also
cloned. We show here that sqh encodes MRLC-C and that in
sqh1 mutants, the level of stable light chain transcript is
greatly reduced. Reversion by transposon excision or
transformation with a wild-type copy of the sqh
transcription unit rescues cytokinesis failure and other
defects in sqh1. Vertebrate homologs of MRLC-C are
phosphorylatable and regulate myosin activity in vitro.
These studies provide genetic proof that MRLC-C is required
for cytokinesis, suggest a role for the protein in
regulating contractile ring function, and establish a
genetic system to evaluate its function.},
Key = {fds153527}
}
@article{fds153528,
Author = {PE Young and TC Pesacreta and DP Kiehart},
Title = {Dynamic changes in the distribution of cytoplasmic myosin
during Drosophila embryogenesis.},
Journal = {Development (Cambridge, England), ENGLAND},
Volume = {111},
Number = {1},
Pages = {1-14},
Year = {1991},
Month = {January},
Keywords = {Animals • Blastoderm • Cytoplasm • Drosophila
melanogaster • Embryo, Nonmammalian • Gastrula
• Microscopy, Immunoelectron • Myosins •
analysis* • chemistry • chemistry* •
ultrastructure},
Abstract = {Dramatic changes in the localization of conventional
non-muscle myosin characterize early embryogenesis in
Drosophila melanogaster. During cellularization, myosin is
concentrated around the furrow canals that form the leading
margin of the plasma membrane as it plunges inward to
package each somatic nucleus into a columnar epithelial
cell. During gastrulation, there is specific anti-myosin
staining at the apical ends of those cells that change shape
in regions of invagination. Both of these localizations
appear to result from a redistribution of a cortical store
of maternal myosin. In the preblastoderm embryo, myosin is
localized to the egg cortex, sub-cortical arrays of
inclusions, and, diffusely, the yolk-free periplasm. At the
syncytial blastoderm stage, myosin is found within
cytoskeletal caps associated with the somatic nuclei at the
embryonic surface. Following the final syncytial division,
these myosin caps give rise to the myosin rings observed
during cellularization. These distributions are observed
with both whole immune serum and affinity-purified
antibodies directed against Drosophila non-muscle myosin
heavy chain. They are not detected in embryos stained with
anti-Drosophila muscle myosin antiserum or with preimmune
serum. Although immunolocalization can only suggest possible
function, these myosin localizations and the coincident
changes in cell morphology are consistent with a key role
for non-muscle myosin in powering cellularization and
gastrulation during embryogenesis.},
Key = {fds153528}
}
@article{fds153529,
Author = {DL Rimm and DA Kaiser and D Bhandari and P Maupin and DP Kiehart and TD
Pollard},
Title = {Identification of functional regions on the tail of
Acanthamoeba myosin-II using recombinant fusion proteins. I.
High resolution epitope mapping and characterization of
monoclonal antibody binding sites.},
Journal = {The Journal of cell biology, UNITED STATES},
Volume = {111},
Number = {6 Pt 1},
Pages = {2405-16},
Year = {1990},
Month = {December},
Keywords = {Acanthamoeba • Animals • Antibodies, Monoclonal
• Antigen-Antibody Complex • Binding Sites •
Cloning, Molecular • DNA • Epitopes •
Immunoblotting • Kinetics • Macromolecular
Substances • Microscopy, Electron • Models,
Structural • Myosins • Recombinant Fusion Proteins
• analysis • diagnostic use • genetics •
metabolism • metabolism* • ultrastructure},
Abstract = {We used a series of COOH-terminally deleted recombinant
myosin molecules to map precisely the binding sites of 22
monoclonal antibodies along the tail of Acanthamoeba
myosin-II. These antibodies bind to 14 distinguishable
epitopes, some separated by less than 10 amino acids. The
positions of the binding sites visualized by electron
microscopy agree only approximately with the physical
positions of these sites on the alpha-helical coiled-coil
tail. On the other hand, the epitope map agrees precisely
with competitive binding studies: all antibodies that share
an epitope compete with each other for binding to myosin.
Antibodies with adjacent epitopes can compete with each
other at linear distances up to 5 or 6 nm, and many
antibodies that bind 3-7-nm apart can enhance the binding of
each other to myosin. Most of the antibodies that bind to
the distal 37 nm of the tail disrupt assembly of octameric
minifilaments and, depending upon the exact location of the
binding site, stop assembly at specific steps yielding, for
example, monomers, antiparallel dimers, parallel dimers or
antiparallel tetramers. The effects of these antibodies on
assembly identify sites on the tail that are required for
individual steps in minifilament assembly. Experiments on
the assembly of truncated myosin-II tails have revealed a
complementary group of sites that participate in the
assembly reactions (Sinard, J.H., D.L. Rimm, and T.D.
Pollard. 1990. J. Cell Biol. 111:2417-2426). Antibodies that
bind to the distal tail but do not affect assembly appear to
have a low affinity for myosin-II. Antibodies that bind to
the proximal 50 nm of the tail do not inhibit the assembly
of minifilaments. Many antibodies that bind to the tail of
myosin-II, even some that have no obvious effect on
minifilament assembly, can inhibit the actomyosin ATPase
activity and the contraction of an actin gel formed in crude
extracts. An antibody that binds between amino acids 1447
and 1467 inhibits the phosphorylation of serine residues
distal to residue 1483.},
Key = {fds153529}
}
@article{fds153530,
Author = {RR Dubreuil and TJ Byers and CT Stewart and DP Kiehart},
Title = {A beta-spectrin isoform from Drosophila (beta H) is similar
in size to vertebrate dystrophin.},
Journal = {The Journal of cell biology, UNITED STATES},
Volume = {111},
Number = {5 Pt 1},
Pages = {1849-58},
Year = {1990},
Month = {November},
Keywords = {Amino Acid Sequence • Animals • Cell Membrane
• Cloning, Molecular • Drosophila •
Dystrophin • Molecular Sequence Data • Molecular
Weight • Sequence Homology, Nucleic Acid •
Spectrin • analysis* • chemistry • isolation
& purification* • ultrastructure},
Abstract = {Spectrins are a major component of the membrane skeleton in
many cell types where they are thought to contribute to cell
form and membrane organization. Diversity among spectrin
isoforms, especially their beta subunits, is associated with
diversity in cell shape and membrane architecture. Here we
describe a spectrin isoform from Drosophila that consists of
a conventional alpha spectrin subunit complexed with a novel
high molecular weight beta subunit (430 kD) that we term
beta H. The native alpha beta H molecule binds actin
filaments with high affinity and has a typical spectrin
morphology except that it is longer than most other spectrin
isoforms and includes two knoblike structures that are
attributed to a unique domain of the beta H subunit. Beta H
is encoded by a different gene than the previously described
Drosophila beta-spectrin subunit but shows sequence
similarity to beta-spectrin as well as vertebrate
dystrophin, a component of the membrane skeleton in muscle.
By size and sequence similarity, dystrophin is more similar
to this newly described beta-spectrin isoform (beta H) than
to other members of the spectrin gene family such as
alpha-spectrin and alpha-actinin.},
Key = {fds153530}
}
@article{fds153531,
Author = {DP Kiehart},
Title = {The actin membrane skeleton in Drosophila
development.},
Journal = {Seminars in cell biology, UNITED STATES},
Volume = {1},
Number = {5},
Pages = {325-39},
Year = {1990},
Month = {October},
Keywords = {Actinin • Actins • Animals • Carrier Proteins
• Cell Compartmentation • Cell Membrane •
Cell Movement • Drosophila melanogaster •
Extracellular Matrix • Microfilament Proteins •
Microfilaments • Myosins • Ovum • Spectrin
• Tropomyosin • embryology* • genetics •
physiology • physiology* • ultrastructure},
Abstract = {Movements, manifest as changes in cell arrangements and
shape, are an integral part of metazoan development. The
molecular basis of such movements is only now being
understood. Drosophila offers an excellent opportunity to
apply powerful classical and modern molecular genetic
methods to the analysis of movements during development.
Moreover, the genes that contribute to pattern formation in
fly development are under intense investigation. The future
promises to illuminate how such genes regulate the structure
and function of the membrane skeleton. This review is a
progress report on our current understanding of the membrane
skeleton in Drosophila.},
Key = {fds153531}
}
@article{fds153532,
Author = {AS Ketchum and CT Stewart and M Stewart and DP Kiehart},
Title = {Complete sequence of the Drosophila nonmuscle myosin
heavy-chain transcript: conserved sequences in the myosin
tail and differential splicing in the 5' untranslated
sequence.},
Journal = {Proceedings of the National Academy of Sciences of the
United States of America, UNITED STATES},
Volume = {87},
Number = {16},
Pages = {6316-20},
Year = {1990},
Month = {August},
Keywords = {Amino Acid Sequence • Animals • Base Sequence
• DNA • Drosophila melanogaster • Gene
Library • Molecular Sequence Data • Myosin
Subfragments • Protein Conformation • RNA
Splicing* • Sequence Homology, Nucleic Acid •
Transcription, Genetic* • genetics •
genetics*},
Abstract = {We have sequenced a cDNA that encodes the nonmuscle myosin
heavy chain from Drosophila melanogaster. An alternatively
spliced exon at the 5' end generates two distinct
heavy-chain transcripts: the longer transcripts inserts an
additional start codon upstream of the primary translation
start site and encodes a myosin heavy chain with a
45-residue extension at its amino terminus. The remainder of
the coding sequence reveals extensive homology with other
conventional myosins, especially metazoan nonmuscle and
smooth muscle myosin isoforms. Comparisons among available
myosin heavy-chain sequences establish that characteristic
differences in sequence throughout the length of both the
globular myosin head and extended rod-like tail readily
distinguish nonmuscle and smooth muscle myosins from
striated muscle isoforms and predict a basis for their
functional diversity.},
Key = {fds153532}
}
@article{fds153533,
Author = {DP Kiehart},
Title = {Molecular genetic dissection of myosin heavy chain
function.},
Journal = {Cell, UNITED STATES},
Volume = {60},
Number = {3},
Pages = {347-50},
Year = {1990},
Month = {February},
Keywords = {Actins • Animals • Cell Division • Cell
Movement • Muscles • Myosin Subfragments •
Myosins • genetics* • metabolism •
physiology},
Key = {fds153533}
}
@article{fds153534,
Author = {DP Kiehart and A Ketchum and P Young and D Lutz and MR Alfenito and XJ
Chang, M Awobuluyi and TC Pesacreta and S Inoué and CT
Stewart},
Title = {Contractile proteins in Drosophila development.},
Journal = {Annals of the New York Academy of Sciences, UNITED
STATES},
Volume = {582},
Pages = {233-51},
Year = {1990},
Keywords = {Actins • Amino Acid Sequence • Animals •
Antibodies, Monoclonal • Base Sequence • Cell
Movement • Contractile Proteins • Cytoskeleton
• DNA • Drosophila • Molecular Sequence Data
• Mutation • Myosins • embryology* •
genetics • immunology • physiology •
physiology*},
Abstract = {In summary, we have used a multidisciplinary approach to the
analysis of actomyosin-based motility during Drosophila
embryogenesis. We have documented the movements of early
embryogenesis with modern, video methods. We have
characterized the cytoplasmic myosin polypeptide, made
specific polyclonal antisera to the molecule, studied its
distribution during early embryogenesis, cloned and
partially characterized the gene that encodes it, and have
recently completed the nucleotide sequence of a nearly full
length cDNA that encodes the entire protein-coding region.
We have initiated studies on myosin function in living
embryos both by direct microinjection of antibodies and
through classical genetics. To better understand how myosin
function is regulated, we have begun analysis of its light
chains. Finally, to investigate the molecular mechanism by
which its function is integrated into a labile cytoskeleton,
whose architecture is constantly changing, we have also
investigated Drosophila spectrins. Together, these studies
are designed to shed light on the dynamics of biologic form
at the cellular level, with current focus on such complex
processes as cytokinesis and morphogenesis.},
Key = {fds153534}
}
@article{fds153535,
Author = {TC Pesacreta and TJ Byers and R Dubreuil and DP Kiehart and D
Branton},
Title = {Drosophila spectrin: the membrane skeleton during
embryogenesis.},
Journal = {The Journal of cell biology, UNITED STATES},
Volume = {108},
Number = {5},
Pages = {1697-709},
Year = {1989},
Month = {May},
Keywords = {Actins • Animals • Antibodies • Blastoderm
• Drosophila melanogaster • Embryo, Nonmammalian
• Fluorescent Antibody Technique • Immunoblotting
• Spectrin • analysis • analysis* •
cytology • embryology* • immunology •
physiology},
Abstract = {The distribution of alpha-spectrin in Drosophila embryos was
determined by immunofluorescence using affinity-purified
polyclonal or monoclonal antibodies. During early
development, spectrin is concentrated near the inner surface
of the plasma membrane, in cytoplasmic islands around the
syncytial nuclei, and, at lower concentrations, throughout
the remainder of the cytoplasm of preblastoderm embryos. As
embryogenesis proceeds, the distribution of spectrin shifts
with the migrating nuclei toward the embryo surface so that,
by nuclear cycle 9, a larger proportion of the spectrin is
concentrated near the plasma membrane. During nuclear cycles
9 and 10, as the nuclei reach the cell surface, the plasma
membrane-associated spectrin becomes concentrated into caps
above the somatic nuclei. Concurrent with the mitotic events
of the syncytial blastoderm period, the spectrin caps
elongate at interphase and prophase, and divide as metaphase
and anaphase progress. During cellularization, the regions
of spectrin concentration appear to shift: spectrin
increases near the growing furrow canal and concomitantly
increases at the embryo surface. In the final phase of
furrow growth, the shift in spectrin concentration is
reversed: spectrin decreases near the furrow canal and
concomitantly increases at the embryo surface. In gastrulae,
spectrin accumulates near the embryo surface, especially at
the forming amnioproctodeal invagination and cephalic
furrow. During the germband elongation stage, the total
amount of spectrin in the embryo increases significantly and
becomes uniformly distributed at the plasma membrane of
almost all cell types. The highest levels of spectrin are in
the respiratory tract cells; the lowest levels are in parts
of the forming gut. The spatial and temporal changes in
spectrin localization suggest that this protein plays a role
in stabilizing rather than initiating changes in structural
organization in the embryo.},
Key = {fds153535}
}
@article{fds153536,
Author = {DP Kiehart and MS Lutz and D Chan and AS Ketchum and RA Laymon and B
Nguyen, LS Goldstein},
Title = {Identification of the gene for fly non-muscle myosin heavy
chain: Drosophila myosin heavy chains are encoded by a gene
family.},
Journal = {The EMBO journal, ENGLAND},
Volume = {8},
Number = {3},
Pages = {913-22},
Year = {1989},
Month = {March},
Keywords = {Amino Acid Sequence • Animals • Cytoplasm •
DNA • Drosophila melanogaster • Gene Expression
Regulation • Genetic Vectors • Molecular Sequence
Data • Multigene Family* • Myosins •
Transcription, Genetic • genetics • genetics*
• metabolism},
Abstract = {In contrast to vertebrate species Drosophila has a single
myosin heavy chain gene that apparently encodes all
sarcomeric heavy chain polypeptides. Flies also contain a
cytoplasmic myosin heavy chain polypeptide that by
immunological and peptide mapping criteria is clearly
different from the major thoracic muscle isoform. Here, we
identify the gene that encodes this cytoplasmic isoform and
demonstrate that it is distinct from the muscle myosin heavy
chain gene. Thus, fly myosin heavy chains are the products
of a gene family. Our data suggest that the contractile
function required to power myosin based movement in
non-muscle cells requires myosin diversity beyond that
available in a single heavy chain gene. In addition, we
show, that accumulation of cytoplasmic myosin transcripts is
regulated in a developmental stage specific fashion,
consistent with a key role for this protein in the movements
of early embryogenesis.},
Key = {fds153536}
}
@article{fds153537,
Author = {R Dubreuil and TJ Byers and D Branton and LS Goldstein and DP
Kiehart},
Title = {Drosophilia spectrin. I. Characterization of the purified
protein.},
Journal = {The Journal of cell biology, UNITED STATES},
Volume = {105},
Number = {5},
Pages = {2095-102},
Year = {1987},
Month = {November},
Keywords = {Actins • Animals • Antibodies • Antibodies,
Monoclonal • Antigen-Antibody Complex • Calmodulin
• Cell Line • Drosophila • Macromolecular
Substances • Microscopy, Electron • Molecular
Weight • Spectrin • isolation & purification*
• metabolism • metabolism*},
Abstract = {We purified a protein from Drosophila S3 tissue culture
cells that has many of the diagnostic features of spectrin
from vertebrate organisms: (a) The protein consists of two
equimolar subunits (Mr = 234 and 226 kD) that can be
reversibly cross-linked into a complex composed of equal
amounts of the two subunits. (b) Electron microscopy of the
native molecule reveals two intertwined, elongated strands
with a contour length of 180 nm. (c) Antibodies directed
against vertebrate spectrin react with the Drosophila
protein and, similarly, antibodies to the Drosophila protein
react with vertebrate spectrins. One monoclonal antibody has
been found to react with both of the Drosophila subunits and
with both subunits of vertebrate brain spectrin. (d) The
Drosophila protein exhibits both actin-binding and
calcium-dependent calmodulin-binding activities. Based on
the above criteria, this protein appears to be a bona fide
member of the spectrin family of proteins.},
Key = {fds153537}
}
@article{fds153538,
Author = {TJ Byers and R Dubreuil and D Branton and DP Kiehart and LS
Goldstein},
Title = {Drosophila spectrin. II. Conserved features of the
alpha-subunit are revealed by analysis of cDNA clones and
fusion proteins.},
Journal = {The Journal of cell biology, UNITED STATES},
Volume = {105},
Number = {5},
Pages = {2103-10},
Year = {1987},
Month = {November},
Keywords = {Animals • Cloning, Molecular* • DNA • DNA
Restriction Enzymes • Drosophila • Genes* •
Macromolecular Substances • Nucleic Acid Hybridization
• Recombinant Proteins • Spectrin • analysis*
• genetics* • isolation & purification},
Abstract = {Drosophila alpha-spectrin cDNA sequences were isolated from
a lambda gt11 expression library. These cDNA clones encode
fusion proteins that include portions of the Drosophila
alpha-spectrin polypeptide as shown by a number of
structural and functional criteria. The fusion proteins
elicited antibodies that reacted strongly with Drosophila
and vertebrate alpha-spectrins and a comparison of cyanogen
bromide peptide maps demonstrated a clear structural
correspondence between one fusion protein and purified
Drosophila alpha-spectrin. Alpha-spectrin fusion protein
also displayed calcium-dependent calmodulin-binding activity
in blot overlay experiments and one fusion protein bound
specifically to both Drosophila and bovine brain
beta-spectrin subunits on protein blots. A region of the
Drosophila cDNA cross-hybridized at lowered stringency with
an avian alpha-spectrin cDNA. Together these data show that
the composition, structure, and binding properties of the
spectrin family of proteins have been remarkably well
conserved between arthropods and vertebrates. Drosophila
cDNA hybridized to an mRNA of greater than or equal to 9 kb
on blots of total Drosophila poly A+ RNA; and hybridized in
situ to a single site in polytene region 62B, 1-7. This
result and Southern blot analysis of genomic DNA indicate
that the sequences are likely to be single copy in the
Drosophila genome.},
Key = {fds153538}
}
@article{fds153539,
Author = {SJ Hagen and DP Kiehart and DA Kaiser and TD Pollard},
Title = {Characterization of monoclonal antibodies to Acanthamoeba
myosin-I that cross-react with both myosin-II and low
molecular mass nuclear proteins.},
Journal = {The Journal of cell biology, UNITED STATES},
Volume = {103},
Number = {6 Pt 1},
Pages = {2121-8},
Year = {1986},
Month = {December},
Keywords = {Amoeba • Animals • Antibodies, Monoclonal •
Antigen-Antibody Complex • Ca(2+) Mg(2+)-ATPase •
Cell Nucleus • Microscopy, Phase-Contrast •
Molecular Weight • Myosins • Nucleoproteins •
analysis • analysis* • cytology* • diagnostic
use* • enzymology • ultrastructure},
Abstract = {We characterized nine monoclonal antibodies that bind to the
heavy chain of Acanthamoeba myosin-IA. Eight of these
antibodies bind to myosin-IB and eight cross-react with
Acanthamoeba myosin-II. All but one of the antibodies bind
to a 30-kD chymotryptic peptide of myosin-IA that derives
from the COOH terminus of the molecule, and to tryptic
peptides as small as 17 kD, hence these epitopes are
clustered closely together on the heavy chain. None of the
antibodies prevent heavy chain phosphorylation by myosin-I
heavy chain kinase. One antibody inhibits the K+-EDTA ATPase
activity and three antibodies inhibit the actin-activated
Mg++-ATPase activity of myosin-I under the set of conditions
that we tested. When fluorescent antibody staining of both
whole cells and isolated nuclei is done, several of these
monoclonal antibodies react strongly with nuclei. These
antibodies also stain the cytoplasmic matrix, especially the
cortex near the plasma membrane. All nine of the monoclonal
antibodies bind to polypeptides of 30-34 kD that are highly
enriched in nuclei isolated from Acanthamoeba. There is no
myosin-I in the isolated nuclei, so the 30-34-kD
polypeptides, not myosin-I, are responsible for the nuclear
staining.},
Key = {fds153539}
}
@article{fds153540,
Author = {DP Kiehart and R Feghali},
Title = {Cytoplasmic myosin from Drosophila melanogaster.},
Journal = {The Journal of cell biology, UNITED STATES},
Volume = {103},
Number = {4},
Pages = {1517-25},
Year = {1986},
Month = {October},
Keywords = {Animals • Antibodies, Monoclonal • Antibody
Specificity • Cell Line • Cytoplasm •
Drosophila melanogaster • Isoenzymes • Muscles
• Myosins • analysis • analysis* •
genetics • immunology • isolation &
purification*},
Abstract = {Myosin is identified and purified from three different
established Drosophila melanogaster cell lines (Schneider's
lines 2 and 3 and Kc). Purification entails lysis in a low
salt, sucrose buffer that contains ATP, chromatography on
DEAE-cellulose, precipitation with actin in the absence of
ATP, gel filtration in a discontinuous KI-KCl buffer system,
and hydroxylapatite chromatography. Yield of pure
cytoplasmic myosin is 5-10%. This protein is identified as
myosin by its cross-reactivity with two monoclonal
antibodies against human platelet myosin, the molecular
weight of its heavy chain, its two light chains, its
behavior on gel filtration, its ATP-dependent affinity for
actin, its characteristic ATPase activity, its molecular
morphology as demonstrated by platinum shadowing, and its
ability to form bipolar filaments. The molecular weight of
the cytoplasmic myosin's light chains and peptide mapping
and immunochemical analysis of its heavy chains demonstrate
that this myosin, purified from Drosophila cell lines, is
distinct from Drosophila muscle myosin. Two-dimensional thin
layer maps of complete proteolytic digests of iodinated
muscle and cytoplasmic myosin heavy chains demonstrate that,
while the two myosins have some tryptic and
alpha-chymotryptic peptides in common, most peptides migrate
with unique mobility. One-dimensional peptide maps of SDS
PAGE purified myosin heavy chain confirm these structural
data. Polyclonal antiserum raised and reacted against
Drosophila myosin isolated from cell lines cross-reacts only
weakly with Drosophila muscle myosin isolated from the
thoraces of adult Drosophila. Polyclonal antiserum raised
against Drosophila muscle myosin behaves in a reciprocal
fashion. Taken together our data suggest that the myosin
purified from Drosophila cell lines is a bona fide
cytoplasmic myosin and is very likely the product of a
different myosin gene than the muscle myosin heavy chain
gene that has been previously identified and
characterized.},
Key = {fds153540}
}
@article{fds153541,
Author = {DP Kiehart and DA Kaiser and TD Pollard},
Title = {Antibody inhibitors of nonmuscle myosin function and
assembly.},
Journal = {Methods in enzymology, UNITED STATES},
Volume = {134},
Pages = {423-53},
Year = {1986},
Keywords = {Animals • Antibodies, Monoclonal* •
Antigen-Antibody Complex* • Electrophoresis,
Polyacrylamide Gel • Enzyme-Linked Immunosorbent Assay
• Immunoglobulin G • Immunoglobulin M •
Isoelectric Focusing • Kinetics • Microscopy,
Electron • Myosins • immunology • isolation &
purification • methods • physiology*},
Key = {fds153541}
}
@article{fds153542,
Author = {AJ Wong and DP Kiehart and TD Pollard},
Title = {Myosin from human erythrocytes.},
Journal = {The Journal of biological chemistry, UNITED
STATES},
Volume = {260},
Number = {1},
Pages = {46-9},
Year = {1985},
Month = {January},
Keywords = {Adenosine Triphosphatases • Antibodies, Monoclonal
• Calcium-Transporting ATPases • Cytosol •
Erythrocytes • Humans • Macromolecular Substances
• Microscopy, Electron • Molecular Weight •
Myosins • analysis • analysis* • blood •
blood* • enzymology • isolation &
purification},
Abstract = {We have purified myosin from human erythrocytes using
methods similar to that for other cytoplasmic myosins with a
yield of about 500 micrograms/100 ml of packed cells. It
consists of a 200-kDa heavy chain and light chains of 26-
and 19.5 kDa and therefore differs from the isozyme in
platelets which has light chains of 20- and 15 kDa. At low
ionic strength, the myosin forms short bipolar filaments
like those of platelet myosin. Eight of eight monoclonal
antibodies to platelet myosin also bind to erythrocyte
myosin. Like most myosins, it has a high ATPase activity in
the presence of Ca2+ or EDTA, but is inhibited by Mg2+.
Myosin light-chain kinase transfers 1 phosphate from ATP to
the 20-kDa light chain, and this stimulates the
actin-activated ATPase. Thus, myosin may play a role in
shape changes in the erythrocytes.},
Key = {fds153542}
}
@article{fds153543,
Author = {A Eisen and DP Kiehart and SJ Wieland and GT Reynolds},
Title = {Temporal sequence and spatial distribution of early events
of fertilization in single sea urchin eggs.},
Journal = {The Journal of cell biology, UNITED STATES},
Volume = {99},
Number = {5},
Pages = {1647-54},
Year = {1984},
Month = {November},
Keywords = {Animals • Calcium • Cytoplasm • Female •
Fertilization* • Luminescent Measurements •
Membrane Potentials • NAD • NADP • Ovum
• Oxidation-Reduction • Sea Urchins •
Spectrometry, Fluorescence • Time Factors •
metabolism • physiology*},
Abstract = {Measurements and observations of five early events of
fertilization, singly and in pairs, from single sea urchin
eggs have revealed the precise temporal sequence and spatial
distribution of these events. In the Arbacia punctulata egg,
a wave of surface contraction occurs coincident with
membrane depolarization (t = 0). These two earliest events
are followed by the onset of a rapid, propagated increase in
cytoplasmic-free calcium at approximately 23 s as measured
by calcium-aequorin luminescence. The luminescence reaches
its peak value by 40 s after the membrane depolarization.
The luminescence remains uniformly elevated for some time
before its decay over several minutes. The onset of an
increase in the pyridine nucleotide (NAD(P)H) fluorescence
follows the membrane depolarization at approximately 51 s.
The fertilization membrane begins its elevation in a
wave-like fashion coincidentally with the increase in
NAD(P)H fluorescence. Similar results are observed in the
Lytechinus variegatus egg. The results suggest that while
the increase in cytoplasmic-free calcium may be important
for many changes occurring in the egg, the elevated-free
calcium is not directly responsible for the propagated wave
of cortical granule exocytosis.},
Key = {fds153543}
}
@article{fds153544,
Author = {DP Kiehart and TD Pollard},
Title = {Inhibition of acanthamoeba actomyosin-II ATPase activity and
mechanochemical function by specific monoclonal
antibodies.},
Journal = {The Journal of cell biology, UNITED STATES},
Volume = {99},
Number = {3},
Pages = {1024-33},
Year = {1984},
Month = {September},
Keywords = {Adenosine Triphosphatases • Amoeba • Animals
• Antibodies • Antibodies, Monoclonal* •
Antigen-Antibody Complex • Electrophoresis,
Polyacrylamide Gel • Epitopes • Kinetics •
Molecular Weight • analysis • antagonists &
inhibitors* • enzymology* • isolation &
purification},
Abstract = {Monoclonal and polyclonal antibodies that bind to myosin-II
were tested for their ability to inhibit myosin ATPase
activity, actomyosin ATPase activity, and contraction of
cytoplasmic extracts. Numerous antibodies specifically
inhibit the actin activated Mg++-ATPase activity of
myosin-II in a dose-dependent fashion, but none blocked the
ATPase activity of myosin alone. Control antibodies that do
not bind to myosin-II and several specific antibodies that
do bind have no effect on the actomyosin-II ATPase activity.
In most cases, the saturation of a single antigenic site on
the myosin-II heavy chain is sufficient for maximal
inhibition of function. Numerous monoclonal antibodies also
block the contraction of gelled extracts of Acanthamoeba
cytoplasm. No polyclonal antibodies tested inhibited ATPase
activity or gel contraction. As expected, most antibodies
that block actin-activated ATPase activity also block gel
contraction. Exceptions were three antibodies M2.2, -15, and
-17, that appear to uncouple the ATPase activity from gel
contraction: they block gel contraction without influencing
ATPase activity. The mechanisms of inhibition of myosin
function depends on the location of the antibody-binding
sites. Those inhibitory antibodies that bind to the
myosin-II heads presumably block actin binding or essential
conformational changes in the myosin heads. A subset of the
antibodies that bind to the proximal end of the myosin-II
tail inhibit actomyosin-II ATPase activity and gel
contraction. Although this part of the molecule is
presumably some distance from the ATP and actin-binding
sites, these antibody effects suggest that structural
domains in this region are directly involved with or coupled
to catalysis and energy transduction. A subset of the
antibodies that bind to the tip of the myosin-II tail appear
to inhibit ATPase activity and contraction through their
inhibition of filament formation. They provide strong
evidence for a substantial enhancement of the ATPase
activity of myosin molecules in filamentous form and suggest
that the myosin filaments may be required for cell
motility.},
Key = {fds153544}
}
@article{fds153545,
Author = {DP Kiehart and DA Kaiser and TD Pollard},
Title = {Direct localization of monoclonal antibody-binding sites on
Acanthamoeba myosin-II and inhibition of filament formation
by antibodies that bind to specific sites on the myosin-II
tail.},
Journal = {The Journal of cell biology, UNITED STATES},
Volume = {99},
Number = {3},
Pages = {1015-23},
Year = {1984},
Month = {September},
Keywords = {Adenosine Triphosphate • Amoeba • Animals •
Antibodies, Monoclonal • Antigen-Antibody Complex
• Binding Sites • Cytoskeleton • Epitopes
• Macromolecular Substances • Microscopy, Electron
• Molecular Weight • Myosins • analysis*
• metabolism • metabolism* •
ultrastructure},
Abstract = {Electron microscopy of myosin-II molecules and filaments
reacted with monoclonal antibodies demonstrates directly
where the antibodies bind and shows that certain antibodies
can inhibit the polymerization of myosin-II into filaments.
The binding sites of seven of 23 different monoclonal
antibodies were localized by platinum shadowing of myosin
monomer-antibody complexes. The antibodies bind to a variety
of sites on the myosin-II molecule, including the heads, the
proximal end of the tail near the junction of the heads and
tail, and the tip of the tail. The binding sites of eight of
the 23 antibodies were also localized on myosin filaments by
negative staining. Antibodies that bind to either the myosin
heads or to the proximal end of the tail decorate the ends
of the bipolar filaments. Some of the antibodies that bind
to the tip of the myosin-II tail decorate the bare zone of
the myosin-II thin filament with 14-nm periodicity. By
combining the data from these electron microscope studies
and the peptide mapping and competitive binding studies we
have established the binding sites of 16 of 23 monoclonal
antibodies. Two of the 23 antibodies block the formation of
myosin-II filaments and given sufficient time, disassemble
preformed myosin-II filaments. Both antibodies bind near one
another at the tip of the myosin-II tail and are those that
decorate the bare zone of preformed bipolar filaments with
14-nm periodicity. None of the other antibodies affect
myosin filament formation, including one that binds to
another site near the tip of the myosin-II tail. This
demonstrates that antibodies can inhibit polymerization of
myosin-II, but only when they bind to key sites on the tail
of the molecule.},
Key = {fds153545}
}
@article{fds153546,
Author = {DP Kiehart and DA Kaiser and TD Pollard},
Title = {Monoclonal antibodies demonstrate limited structural
homology between myosin isozymes from Acanthamoeba.},
Journal = {The Journal of cell biology, UNITED STATES},
Volume = {99},
Number = {3},
Pages = {1002-14},
Year = {1984},
Month = {September},
Keywords = {Amoeba • Animals • Antibodies, Monoclonal •
Electrophoresis, Polyacrylamide Gel • Epitopes •
Isoenzymes • Molecular Weight • Myosins •
Peptide Fragments • Trypsin • analysis •
analysis* • genetics • metabolism*},
Abstract = {We used a library of 31 monoclonal and six polyclonal
antibodies to compare the structures of the two classes of
cytoplasmic myosin isozymes isolated from Acanthamoeba:
myosin-I, a 150,000-mol-wt, globular molecule; and
myosin-II, a 400,000-mol-wt molecule with two heads and a
90-nm tail. This analysis confirms that myosin-I and -II are
unique gene products and provides the first evidence that
these isozymes have at least one structurally homologous
region functionally important for myosin's role in
contractility. Characterization of the 23 myosin-II
monoclonal antibody binding sites by antibody staining of
one-dimensional peptide maps and solid phase, competitive
binding assays demonstrate that they bind to at least 15
unique sites on the myosin-II heavy chain. The antibodies
can be grouped into six families, whose members bind close
to one another. None of the monoclonal antibodies bind to
myosin-II light chains and polyclonal antibodies against
myosin-II light or heavy chain bind only to myosin-II light
or heavy chains, respectively: no antibody binds both heavy
and light chains. Six of eight monoclonal antibodies and one
of two polyclonal sera that react with the myosin-I heavy
chain also bind to determinants on the myosin-II heavy
chain. The cross-reactive monoclonal antibodies bind to the
region of myosin-II recognized by the largest family of
myosin-II monoclonal antibodies. In the two papers that
immediately follow, we show that this family of monoclonal
antibodies to myosin-II binds to the myosin-II tail near the
junction with the heads and inhibits both the
actin-activated ATPase of myosin-II and contraction of
gelled cytoplasmic extracts of Acanthamoeba cytoplasm.
Further, this structurally homologous region may play a key
role in energy transduction by cytoplasmic
myosins.},
Key = {fds153546}
}
@article{fds153547,
Author = {TD Pollard and U Aebi and JA Cooper and WE Fowler and DP Kiehart and PR
Smith, PC Tseng},
Title = {Actin and myosin function in acanthamoeba.},
Journal = {Philosophical transactions of the Royal Society of London.
Series B, Biological sciences, ENGLAND},
Volume = {299},
Number = {1095},
Pages = {237-45},
Year = {1982},
Month = {November},
Keywords = {Actins • Amoeba • Animals • Antibodies,
Monoclonal • Macromolecular Substances •
Microinjections • Microscopy, Electron • Myosins
• Polymers • physiology • physiology* •
ultrastructure*},
Abstract = {We have studied the functions of contractile proteins in
Acanthamoeba by a combination of structural, biochemical and
physiological approaches. We used electron microscopy and
image processing to determine the three-dimensional
structure of actin and the orientation of the molecule in
the actin filament. We measured the rate constants for actin
filament elongation and re-evaluated the effect of MgCl2 on
the filament nucleation process. In Acanthamoeba actin
polymerization is regulated, at least in part, by profilin,
which binds to actin monomers, and by capping protein, which
both nucleates polymerization and blocks monomer addition at
the 'barbed' end of the filament. To test for physiological
functions of myosin-II, we produced a monoclonal antibody
that inhibits the actin-activated ATPase. When microinjected
into living cells, this active-site-specific antibody
inhibits amoeboid locomotion. We expect that similar
experiments can be used to test for the physiological
functions of the other components of the Acanthamoeba
contractile system.},
Key = {fds153547}
}
@article{fds153548,
Author = {DP Kiehart and I Mabuchi and S Inoué},
Title = {Evidence that myosin does not contribute to force production
in chromosome movement.},
Journal = {The Journal of cell biology, UNITED STATES},
Volume = {94},
Number = {1},
Pages = {165-78},
Year = {1982},
Month = {July},
Keywords = {Actins • Adenosine Triphosphatases • Anaphase
• Blastomeres • Ca(2+) Mg(2+)-ATPase • Cell
Division • Cell Nucleus • Chromosomes •
Cleavage Stage, Ovum • Fertilization • Meiosis
• Mitosis • Myosins • Starfish •
gamma-Globulins • metabolism • metabolism* •
physiology*},
Abstract = {Antibody against cytoplasmic myosin, when microinjected into
actively dividing cells, provides a physiological test for
the role of actin and myosin in chromosome movement.
Anti-Asterias egg myosin, characterized by Mabuchi and Okuno
(1977, J. Cell Biol., 74:251), completely and specifically
inhibits the actin activated Mg++ -ATPase of myosin in vitro
and, when microinjected, inhibits cytokinesis in vivo. Here,
we demonstrate that microinjected antibody has no observable
effect on the rate or extent of anaphase chromosome
movements. Neither central spindle elongation nor
chromosomal fiber shortening is affected by doses up to
eightfold higher than those require to uniformly inhibit
cytokinesis in all injected cells. We calculate that such
doses are sufficient to completely inhibit myosin ATPase
activity in these cells. Cells injected with buffer alone,
with myosin-absorbed antibody, or with nonimmune
gamma-globulin, proceed normally through both mitosis and
cytokinesis. Control gamma-globulin, labeled with
fluorescein, diffuses to homogeneity throughout the
cytoplasm in 2-4 min and remains uniformly distributed.
Antibody is not excluded from the spindle region.
Prometaphase chromosome movements, fertilization, pronuclear
migration, and pronuclear fusion are also unaffected by
microinjected antimyosin. These experiments demonstrate that
antimyosin blocks the actomyosin interaction thought to be
responsible for force production in cytokinesis but has no
effect on mitotic or meiotic chromosome motion. They provide
direct physiological evidence that myosin is not involved in
force production for chromosome movement.},
Key = {fds153548}
}
@article{fds153549,
Author = {DP Kiehart},
Title = {Microinjection of echinoderm eggs: apparatus and
procedures.},
Journal = {Methods in cell biology, UNITED STATES},
Volume = {25 Pt B},
Pages = {13-31},
Year = {1982},
Keywords = {Animals • Echinodermata • Female •
Microinjections • Ovum • cytology* • methods*
• ultrastructure*},
Key = {fds153549}
}
@article{fds153550,
Author = {DP Kiehart},
Title = {Studies on the in vivo sensitivity of spindle microtubules
to calcium ions and evidence for a vesicular
calcium-sequestering system.},
Journal = {The Journal of cell biology, UNITED STATES},
Volume = {88},
Number = {3},
Pages = {604-17},
Year = {1981},
Month = {March},
Keywords = {Animals • Birefringence • Caffeine • Calcium
• Female • Microinjections • Microtubules
• Mitosis* • Oxalates • Sea Urchins •
Starfish • Zygote • drug effects* •
metabolism • pharmacology • pharmacology*},
Abstract = {I microinjected calcium ions into echinoderm eggs during
mitosis to determine the calcium sensitivity of microtubules
(Mts) in vivo. Spindle birefringence (BR), a measure of the
number of aligned Mts in the spindle, is locally, rapidly,
and reversibly abolished by small volumes of microinjected
CaCl2 (1 mM). Rapid return of BR is followed by anaphase,
and subsequent divisions are normal. Similar doses of MgCl2,
BaCl2, KCl, NaCl, pH buffers, distilled water, or vegetable
oil have no effect on spindle BR, whereas large doses of
such agents sometimes cause slow, uniform loss in BR over
the course of a minute or more. Of the ions tested, only
Sr++ causes effects comparable to Ca++. Ca-EGTA buffers,
containing greater than micromolar free Ca++, abolishes BR
in a manner similar to millimolar concentrations of injected
CaCl2. Caffeine, a potent uncoupler of the Ca++-pump/ATPase
of sarcoplasmic reticulum, causes a local, transient
depression in spindle BR in the injected region. Finally,
injection of potassium oxalate results in the formation of
small, highly BR crystals, presumably CA-oxalate, in
Triton-sensitive compartments in the cytoplasm. Taken
together, these findings demonstrate that spindle Mts are
sensitive to levels of free Ca++ in the physiological range,
provide evidence for the existence of a strong cytoplasmic
Ca++-sequestering system, and support the notion that Mt
assembly and disassembly in local regions of the spindle may
be orchestrated by local changes in the cytoplasmic free
Ca++ concentration during mitosis. An appendix offers the
design of a new chamber for immobilizing echinoderm eggs for
injection, a new method for determining the volume of the
injected solution, and a description of the microinjection
technique, which was designed, but never fully described, by
Hiramoto (Y. Hiramoto, Exp. Cell. Res., 1962,
27:416-426.).},
Key = {fds153550}
}
@article{fds153551,
Author = {LG Tilney and DP Kiehart and C Sardet and M Tilney},
Title = {Polymerization of actin. IV. Role of Ca++ and H+ in the
assembly of actin and in membrane fusion in the acrosomal
reaction of echinoderm sperm.},
Journal = {The Journal of cell biology, UNITED STATES},
Volume = {77},
Number = {2},
Pages = {536-50},
Year = {1978},
Month = {May},
Keywords = {Acrosome • Actins* • Animals • Calcium •
Echinodermata • Hydrogen • Hydrogen-Ion
Concentration • Ionophores • Male • Polymers
• Spermatozoa • drug effects • metabolism*
• pharmacology • physiology •
ultrastructure*},
Abstract = {When Pisaster, Asterias, or Thyone sperm are treated with
the ionophore A23187 or X537A, an acrosomal reaction similar
but not identical to a normal acrosomal reaction is induced
in all the sperm. Based upon the response of the sperm, the
acrosomal reaction consists of a series of temporally
related steps. These include the fusion of the acrosomal
vacuole with the cell surface, the polymerization of the
actin, the alignment of the actin filaments, an increase in
volume, an increase in the limiting membrane, and changes in
the shape of the nucleus. In this report, we have
concentrated on the first two steps in this sequence.
Although fusion of the acrosomal vacuole with the cell
surface requires Ca++, we found that the polymerization of
actin instead appears to be dependent upon an increase in
intracellular pH. This conclusion was reached by applying to
sperm A23187, X537A, or nigericin, ionophores which all
carry H+ at high affinity, yet vary in their affinity for
other cations. When sperm are suspended in isotonic NaCl,
isotonic KCl, calcium-free seawater, or seawater, all at pH
8.0, and the ionophore is added, the actin polymerizes
explosively and an efflux of H+ from the cell occurs.
However, if the pH, of the external medium is maintained at
6.5, the presumed intracellular pH, no effect is observed.
And, finally, if egg jelly is added to sperm (the natural
stimulus for the acrosomal reaction) at pH 8.0, H+ is also
released. On the basis of these observations and those
presented in earlier papers in this series, we conclude that
a rise in intracellular pH induces the actin to disassociate
from its binding proteins. Now it can polymerize.},
Key = {fds153551}
}
@article{fds153552,
Author = {S Inoué and GG Borisy and DP Kiehart},
Title = {Growth and lability of Chaetopterus oocyte mitotic spindles
isolated in the presence of porcine brain
tubulin.},
Journal = {The Journal of cell biology, UNITED STATES},
Volume = {62},
Number = {1},
Pages = {175-84},
Year = {1974},
Month = {July},
Keywords = {Animals • Birefringence • Brain • Buffers
• Colchicine • Cold Temperature • Cytoplasm
• Demecolcine • Drug Stability • Evaluation
Studies as Topic • Female • Insects • Methods
• Mitosis* • Nerve Tissue Proteins* • Ovum
• Swine • Time Factors • cytology* •
metabolism},
Key = {fds153552}
}
@article{fds153498,
Author = {D Dutta and JW Bloor and M Ruiz-Gomez and K VijayRaghavan and DP
Kiehart},
Title = {Real-time imaging of morphogenetic movements in Drosophila
using Gal4-UAS-driven expression of GFP fused to the
actin-binding domain of moesin.},
Journal = {Genesis (New York, N.Y. : 2000), United States},
Volume = {34},
Number = {1-2},
Pages = {146-51},
Keywords = {Actins • Animals • Animals, Genetically Modified
• Binding Sites • Drosophila melanogaster •
Enhancer Elements, Genetic* • Green Fluorescent
Proteins • Larva • Luminescent Proteins •
Microfilament Proteins • Molecular Sequence Data •
Pupa • Saccharomyces cerevisiae Proteins •
Staining and Labeling • Transcription Factors •
embryology • genetics* • metabolism},
Key = {fds153498}
}
@article{ISI:A1986E958900435,
Author = {KIEHART, DP and SAFT, MS and LAYMON, RA and GOLDSTEIN, LSB and OBRIEN, J},
Title = {{IDENTIFICATION AND PARTIAL CHARACTERIZATION OF A PORTION OF
THE CODING SEQUENCE FOR CYTOPLASMIC MYOSIN IN
DROSOPHILA}},
Journal = {{JOURNAL OF CELL BIOLOGY}},
Volume = {{103}},
Number = {{5, Part 2}},
Pages = {{A115}},
ISSN = {{0021-9525}},
Key = {ISI:A1986E958900435}
}
@article{ISI:A1977CU58800486,
Author = {MOOSEKER, MS and PRATT, M and KIEHART, DP and STEPHENS,
RE},
Title = {{CYCLIC CONTRACTION AND RELAXATION OF SARCOMERES IN ISOLATED
MYOFIBRILS}},
Journal = {{BIOPHYSICAL JOURNAL}},
Volume = {{17}},
Number = {{2}},
Pages = {{A173}},
ISSN = {{0006-3495}},
Key = {ISI:A1977CU58800486}
}
@article{ISI:A1989U846900034,
Author = {KIEHART, DP},
Title = {{CORRECTION}},
Journal = {{EMBO JOURNAL}},
Volume = {{8}},
Number = {{6}},
Pages = {{1896}},
ISSN = {{0261-4189}},
Key = {ISI:A1989U846900034}
}
@article{ISI:A1981NT31301131,
Author = {KIEHART, DP and KAISER, DA and POLLARD, TD},
Title = {{MONOCLONAL-ANTIBODIES TO ACANTHAMOEBA MYOSINS}},
Journal = {{JOURNAL OF CELL BIOLOGY}},
Volume = {{91}},
Number = {{2}},
Pages = {{A299}},
ISSN = {{0021-9525}},
Key = {ISI:A1981NT31301131}
}
@article{ISI:A1975AU24800042,
Author = {KIEHART, DP and INOUE, S},
Title = {{MICROTUBULE DEPOLYMERIZATION IN LOCAL REGIONS OF MITOTIC
SPINDLE BY CA++ MICROINJECTION}},
Journal = {{BIOLOGICAL BULLETIN}},
Volume = {{149}},
Number = {{2}},
Pages = {{433}},
ISSN = {{0006-3185}},
Key = {ISI:A1975AU24800042}
}
@article{ISI:A1981LE20200015,
Author = {KIEHART, DP},
Title = {{STUDIES ON THE INVIVO SENSITIVITY OF SPINDLE MICROTUBULES
TO CALCIUM-IONS AND EVIDENCE FOR A VESICULAR
CALCIUM-SEQUESTERING SYSTEM}},
Journal = {{JOURNAL OF CELL BIOLOGY}},
Volume = {{88}},
Number = {{3}},
Pages = {{604-617}},
ISSN = {{0021-9525}},
Key = {ISI:A1981LE20200015}
}
@article{ISI:000244166400001,
Author = {Kiehart, Daniel P. and Bloom, Kerry},
Title = {{Cell structure and dynamics - Editorial
overview}},
Journal = {{CURRENT OPINION IN CELL BIOLOGY}},
Volume = {{19}},
Number = {{1}},
Pages = {{1-4}},
ISSN = {{0955-0674}},
Key = {ISI:000244166400001}
}
@article{ISI:000224648803299,
Author = {Peralta, XG and Toyama, Y and Wells, A and Tokutake, Y and Hutson, MS and Venakides, S and Kiehart, DP and Edwards,
GS},
Title = {{Force regulation during dorsal closure in
Drosophila}},
Journal = {{MOLECULAR BIOLOGY OF THE CELL}},
Volume = {{15}},
Number = {{Suppl. S}},
Pages = {{403A}},
ISSN = {{1059-1524}},
Key = {ISI:000224648803299}
}
@article{ISI:000225997100032,
Author = {Franke, JD and Dong, F and Rickoll, WL and Kelley, MJ and Kiehart, DP},
Title = {{Rod mutations associated with MYH9-related disorders
disrupt nonmuscle myosin-IIA assembly}},
Journal = {{BLOOD}},
Volume = {{105}},
Number = {{1}},
Pages = {{161-169}},
ISSN = {{0006-4971}},
Abstract = {{MYH9-related disorders are autosomal dominant syndromes,
variably affecting platelet formation, hearing, and kidney
function, and result from mutations in the human nonmuscle
myosin-IIA heavy chain gene. To understand the mechanisms by
which mutations in the rod region disrupt nonmuscle
myosin-IIA function, we examined the in vitro behavior of 4
common mutant forms of the rod(R1165C, D1424N, E1841K, and
R1933Stop) compared with wild type. We used negative-stain
electron microscopy to analyze paracrystal morphology, a
model system for the assembly of individual myosin-II
molecules into bipolar filaments. Wild-type tail fragments
formed ordered paracrystal arrays, whereas mutants formed
aberrant aggregates. In mixing experiments, the mutants act
dominantly to interfere with the proper assembly of wild
type. Using circular dichroism, we find that 2 mutants
affect the alpha-helical coiled-coil structure of individual
molecules, and 2 mutants disrupt the lateral associations
among individual molecules necessary to form higher-order
assemblies, helping explain the dominant effects of these
mutants. These results demonstrate that the most common
mutations in MYH9, lesions in the rod, cause defects in
nonmuscle myosin-IIA assembly. Further, the application of
these methods to biochemically characterize rod mutations
could be extended to other myosins responsible for disease.
(Blood. 2005;105:161-169) (C) 2005 by The American Society
of Hematology.}},
Key = {ISI:000225997100032}
}
@article{ISI:A1983RR86600083,
Author = {EISEN, A and REYNOLDS, GT and WIELAND, S and KIEHART,
DP},
Title = {{CALCIUM TRANSIENTS DURING FERTILIZATION IN SINGLE
SEA-URCHIN EGGS}},
Journal = {{BIOLOGICAL BULLETIN}},
Volume = {{165}},
Number = {{2}},
Pages = {{514-515}},
ISSN = {{0006-3185}},
Key = {ISI:A1983RR86600083}
}
@article{ISI:A1986A176800209,
Author = {KETCHUM, AS and KIEHART, DP},
Title = {{PROFILIN FROM DROSOPHILA}},
Journal = {{BIOPHYSICAL JOURNAL}},
Volume = {{49}},
Number = {{2, Part 2}},
Pages = {{A75}},
ISSN = {{0006-3495}},
Key = {ISI:A1986A176800209}
}
@article{ISI:A1982PN30201243,
Author = {KIEHART, DP and KAISER, DA and FOWLER, WE and POLLARD,
TD},
Title = {{MONOCLONAL-ANTIBODIES PROBE MYOSIN FUNCTION-INVITRO AND
INVIVO}},
Journal = {{JOURNAL OF CELL BIOLOGY}},
Volume = {{95}},
Number = {{2}},
Pages = {{A326}},
ISSN = {{0021-9525}},
Key = {ISI:A1982PN30201243}
}
@article{ISI:A1992JR25500896,
Author = {EDWARDS, KA and SHEPARD, S and EDGAR, B and ERIKSON, RL and KIEHART, DP},
Title = {{IDENTIFICATION OF CDNAS ENCODING DROSOPHILA CYTOSKELETAL
ELEMENTS BY FUNCTIONAL EXPRESSION CLONING IN
SCHIZOSACCHAROMYCES-POMBE}},
Journal = {{MOLECULAR BIOLOGY OF THE CELL}},
Volume = {{3}},
Number = {{Suppl. S}},
Pages = {{A154}},
ISSN = {{1059-1524}},
Key = {ISI:A1992JR25500896}
}
@article{ISI:A1995TF51302336,
Author = {THOMAS, GH and KIEHART, DP},
Title = {{BETA((HEAVY))-SPECTRIN IS POLARIZED IN THE MEMBRANE
SKELETON AND ESSENTIAL FOR DROSOPHILA DEVELOPMENT}},
Journal = {{MOLECULAR BIOLOGY OF THE CELL}},
Volume = {{6}},
Number = {{Suppl. S}},
Pages = {{2336}},
ISSN = {{1059-1524}},
Key = {ISI:A1995TF51302336}
}
@article{ISI:A1996WB01801146,
Author = {Su, Z and Kiehart, DP},
Title = {{Phosphorylation of Drosophila nonmuscle myosin II heavy
chain by Protein Kinase C, Casein Kinase II and a putative
myosin heavy chain kinase.}},
Journal = {{MOLECULAR BIOLOGY OF THE CELL}},
Volume = {{7}},
Number = {{Suppl. S}},
Pages = {{1148}},
ISSN = {{1059-1524}},
Key = {ISI:A1996WB01801146}
}
@article{ISI:000076906700847,
Author = {Bloor, JW and Kiehart, DP},
Title = {{Nonsarcomeric myosin II, PS2 integrin and
myogenesis.}},
Journal = {{MOLECULAR BIOLOGY OF THE CELL}},
Volume = {{9}},
Number = {{Suppl. S}},
Pages = {{146A}},
ISSN = {{1059-1524}},
Key = {ISI:000076906700847}
}
@article{ISI:A1987L083700016,
Author = {DUBREUIL, R and BYERS, TJ and BRANTON, D and GOLDSTEIN, LSB and KIEHART, DP},
Title = {{DROSOPHILA SPECTRIN .1. CHARACTERIZATION OF THE PURIFIED
PROTEIN}},
Journal = {{JOURNAL OF CELL BIOLOGY}},
Volume = {{105}},
Number = {{5}},
Pages = {{2095-2102}},
ISSN = {{0021-9525}},
Key = {ISI:A1987L083700016}
}
@article{ISI:A1976CJ96300073,
Author = {PRATT, MM and MOOSEKER, MS and KIEHART, DP and STEPHENS,
RE},
Title = {{CYCLIC CONTRACTION AND RELAXATION OF GLYCERINATED
MYOFIBRILS ISOLATED FROM SKELETAL-MUSCLE}},
Journal = {{BIOLOGICAL BULLETIN}},
Volume = {{151}},
Number = {{2}},
Pages = {{426}},
ISSN = {{0006-3185}},
Key = {ISI:A1976CJ96300073}
}
@article{ISI:000074281900336,
Author = {Bloor, JW and Kiehart, DP},
Title = {{The role of nonsarcomeric myosin in Drosophila
myogenesis.}},
Journal = {{DEVELOPMENTAL BIOLOGY}},
Volume = {{198}},
Number = {{1}},
Pages = {{215}},
ISSN = {{0012-1606}},
Key = {ISI:000074281900336}
}
@article{ISI:A1996TZ28400501,
Author = {Somjen, GG and Wadman, WJ and Juta, A and Borgdorf, A and Aitken, PG and Kiehart, DP},
Title = {{Osmotically induced volume changes of freshly isolated rat
hippocampal neurons.}},
Journal = {{FASEB JOURNAL}},
Volume = {{10}},
Number = {{3}},
Pages = {{500}},
ISSN = {{0892-6638}},
Key = {ISI:A1996TZ28400501}
}
@article{ISI:000172372501635,
Author = {Wiemann, JM and Franke, JD and Kiehart, DP},
Title = {{RhoA is required for actomyosin purse string contractility
in Drosophila wound healing}},
Journal = {{MOLECULAR BIOLOGY OF THE CELL}},
Volume = {{12}},
Number = {{Suppl. S}},
Pages = {{299A}},
ISSN = {{1059-1524}},
Key = {ISI:000172372501635}
}
@article{ISI:A1984SN80100088,
Author = {KIEHART, DP and POLLARD, TD},
Title = {{STIMULATION OF ACANTHAMOEBA ACTOMYOSIN ATPASE ACTIVITY BY
MYOSIN-II POLYMERIZATION}},
Journal = {{NATURE}},
Volume = {{308}},
Number = {{5962}},
Pages = {{864-866}},
ISSN = {{0028-0836}},
Key = {ISI:A1984SN80100088}
}
@article{ISI:000224648803072,
Author = {Todi, SV and Franke, JD and Kiehart, DP and Eberl,
DF},
Title = {{Myosin VIIa is important structurally and physiologically
for drosophila auditory mechanotransduction}},
Journal = {{MOLECULAR BIOLOGY OF THE CELL}},
Volume = {{15}},
Number = {{Suppl. S}},
Pages = {{362A}},
ISSN = {{1059-1524}},
Key = {ISI:000224648803072}
}
@article{ISI:000240671200002,
Author = {Franke, Josef D. and Boury, Amanda L. and Gerald, Noel J. and Kiehart, Daniel P.},
Title = {{Native nonmuscle myosin II stability and light chain
binding in Drosophila melanogaster}},
Journal = {{CELL MOTILITY AND THE CYTOSKELETON}},
Volume = {{63}},
Number = {{10}},
Pages = {{604-622}},
ISSN = {{0886-1544}},
Abstract = {{Native nonmuscle myosin IIs play essential roles in
cellular and developmental processes throughout phylogeny.
Individual motor molecules consist of a hetero-hexameric
complex of three polypeptides which, when properly
assembled, are capable of force generation. Here, we more
completely characterize the properties, relationships and
associations that each subunit has with one another in
Drosophila melanogaster. All three native nonmuscle myosin
11 polypeptide subunits are expressed in close to constant
stoichiometry to each other throughout development. We find
that the stability of two subunits, the heavy chain and the
regulatory light chain, depend on one another whereas the
stability of the third subunit, the essential light chain,
does not depend on either the heavy chain or regulatory
light chain. We demonstrate that heavy chain aggregates,
which form in when regulatory light chain is lacking,
associate with the essential light chain vivo-thus showing
that regulatory light chain association is required for
heavy chain solubility. By immunodepletion we find that the
majority of both light chains are associated with the
nonmuscle myosin 11 heavy chain but pools of free light
chain and/or light chain bound to other proteins are
present. We identify four myosins (myosin 11, myosin V,
myosin VI and myosin VIIA) and a microtubule-associated
protein (asp/Abnormal spindle) as binding partners for the
essential light chain (but not the regulatory light chain)
through mass spectrometry and co-precipitation. Using an in
silico approach we identify six previously uncharacterized
genes that contain IQ-motifs and may be essential light
chain binding partners.}},
Key = {ISI:000240671200002}
}
@article{ISI:000076906700824,
Author = {Alcorta, DA and Montague, RA and Edwards, KA and Kiehart,
DP},
Title = {{GFP-moesin fusion proteins function as real-time markers of
actin cable reorganization in cultured cells.}},
Journal = {{MOLECULAR BIOLOGY OF THE CELL}},
Volume = {{9}},
Number = {{Suppl. S}},
Pages = {{142A}},
ISSN = {{1059-1524}},
Key = {ISI:000076906700824}
}
@article{ISI:A1980JP62702983,
Author = {KIEHART, DP and POLLARD, TD},
Title = {{A MONOCLONAL-ANTIBODY TO MYOSIN}},
Journal = {{FEDERATION PROCEEDINGS}},
Volume = {{39}},
Number = {{6}},
Pages = {{2167}},
ISSN = {{0014-9446}},
Key = {ISI:A1980JP62702983}
}
@article{ISI:A1983RR86600082,
Author = {EISEN, A and REYNOLDS, GT and WIELAND, S and KIEHART,
DP},
Title = {{CALCIUM TRANSIENTS DURING FERTILIZATION IN SINGLE
SEA-URCHIN EGGS}},
Journal = {{BIOLOGICAL BULLETIN}},
Volume = {{165}},
Number = {{2}},
Pages = {{514}},
ISSN = {{0006-3185}},
Key = {ISI:A1983RR86600082}
}
@article{ISI:A1982ND35600112,
Author = {KIEHART, DP and KAISER, DA and POLLARD, TD},
Title = {{MONOCLONAL-ANTIBODIES INHIBIT THE ACTIN ACTIVATED
MG++-ATPASE OF ACANTHAMOEBA MYOSIN II}},
Journal = {{BIOPHYSICAL JOURNAL}},
Volume = {{37}},
Number = {{2}},
Pages = {{A40}},
ISSN = {{0006-3495}},
Key = {ISI:A1982ND35600112}
}
@article{ISI:000227610701366,
Author = {Kiehart, D},
Title = {{Imaging Drosophila development}},
Journal = {{FASEB JOURNAL}},
Volume = {{19}},
Number = {{4, Part 1 Suppl. S}},
Pages = {{A217}},
ISSN = {{0892-6638}},
Key = {ISI:000227610701366}
}
@article{ISI:A1978EP90300728,
Author = {INOUE, S and KIEHART, DP},
Title = {{INVIVO ANALYSIS OF MITOTIC SPINDLE DYNAMICS}},
Journal = {{JOURNAL OF SUPRAMOLECULAR STRUCTURE}},
Number = {{Suppl. 2}},
Pages = {{290}},
ISSN = {{0091-7419}},
Key = {ISI:A1978EP90300728}
}
@article{ISI:A1995TF51300014,
Author = {EDWARDS, K and DEMSKY, M and KIEHART, DP},
Title = {{A GFP-MOESIN FUSION PROVIDES A NOVEL TOOL TO STUDY CHANGES
IN CELL MORPHOLOGY}},
Journal = {{MOLECULAR BIOLOGY OF THE CELL}},
Volume = {{6}},
Number = {{Suppl. S}},
Pages = {{12}},
ISSN = {{1059-1524}},
Key = {ISI:A1995TF51300014}
}
@article{ISI:A1984TM94900127,
Author = {HAGEN, SC and KIEHART, DP and KAISER, DA and POLLARD,
TD},
Title = {{MONOCLONAL-ANTIBODIES AS PROBES TO THE STRUCTURE AND
FUNCTION OF MYOSIN-I IN ACANTHAMOEBA}},
Journal = {{JOURNAL OF CELL BIOLOGY}},
Volume = {{99}},
Number = {{4}},
Pages = {{A35}},
ISSN = {{0021-9525}},
Key = {ISI:A1984TM94900127}
}
@article{ISI:000076906702254,
Author = {Kiehart, DP and Montague, RA and Roote, J and Ashburner,
M},
Title = {{Evidence that crinkled, mutations in which cause numerous
defects in Drosophila morphogenesis, encodes a myosin
VII.}},
Journal = {{MOLECULAR BIOLOGY OF THE CELL}},
Volume = {{9}},
Number = {{Suppl. S}},
Pages = {{388A}},
ISSN = {{1059-1524}},
Key = {ISI:000076906702254}
}
@article{ISI:000089209800039,
Author = {Halsell, SR and Chu, BI and Kiehart, DP},
Title = {{Genetic analysis demonstrates a direct link between rho
signaling and nonmuscle myosin function during drosophila
morphogenesis (vol 155, pg 1253, 2000)}},
Journal = {{GENETICS}},
Volume = {{156}},
Number = {{1}},
Pages = {{469}},
ISSN = {{0016-6731}},
Key = {ISI:000089209800039}
}
@article{ISI:A1992JR25500258,
Author = {MANSFIELD, SG and YOUNG, PE and KIEHART,
DP},
Title = {{THE GENOMIC DNA-STRUCTURE OF THE DROSOPHILA CYTOPLASMIC
MYOSIN HEAVY-CHAIN GENE}},
Journal = {{MOLECULAR BIOLOGY OF THE CELL}},
Volume = {{3}},
Number = {{Suppl. S}},
Pages = {{A45}},
ISSN = {{1059-1524}},
Key = {ISI:A1992JR25500258}
}
@article{ISI:000179569101007,
Author = {Franke, JD and Kiehart, DP},
Title = {{New probes for the role of non-muscle myosin II during
development}},
Journal = {{MOLECULAR BIOLOGY OF THE CELL}},
Volume = {{13}},
Pages = {{180A}},
ISSN = {{1059-1524}},
Key = {ISI:000179569101007}
}
@article{ISI:A1996WB01800202,
Author = {Halsell, SR and Kiehart, DP},
Title = {{Identification of in vivo interactions with Drosophila
nonmuscle myosin.}},
Journal = {{MOLECULAR BIOLOGY OF THE CELL}},
Volume = {{7}},
Number = {{Suppl. S}},
Pages = {{202}},
ISSN = {{1059-1524}},
Key = {ISI:A1996WB01800202}
}
@article{ISI:000076906701648,
Author = {Crawford, JM and Harden, N and Leung, T and Lim, L and Kiehart, DP},
Title = {{Cellularization in Drosophila melanogaster is regulated by
the Rho subfamily signaling cascades}},
Journal = {{MOLECULAR BIOLOGY OF THE CELL}},
Volume = {{9}},
Number = {{Suppl. S}},
Pages = {{284A}},
ISSN = {{1059-1524}},
Key = {ISI:000076906701648}
}
@article{ISI:A1992JR25500901,
Author = {THOMAS, GH and KIEHART, DP},
Title = {{MUTATIONS IN THE KARST (KST) GENE OF DROSOPHILA-MELANOGASTER
ALTER THE BETAHEAVY-SPECTRIN PROTEIN AND DISRUPT
DEVELOPMENT}},
Journal = {{MOLECULAR BIOLOGY OF THE CELL}},
Volume = {{3}},
Number = {{Suppl. S}},
Pages = {{A155}},
ISSN = {{1059-1524}},
Key = {ISI:A1992JR25500901}
}
@article{ISI:A1981NT31301336,
Author = {HERMAN, IM and STOECKERT, C and KIEHART, DP and WIGGINS, W and BEER, M and POLLARD, TD},
Title = {{COVALENT MODIFICATION OF ANTI-MYOSIN WITH HEAVY-ATOMS FOR
USE IN STEM}},
Journal = {{JOURNAL OF CELL BIOLOGY}},
Volume = {{91}},
Number = {{2}},
Pages = {{A353}},
ISSN = {{0021-9525}},
Key = {ISI:A1981NT31301336}
}
@article{ISI:000181988900053,
Author = {Hutson, MS and Tokutake, Y and Chang, MS and Bloor, JW and Venakides, S and Kiehart, DP and Edwards,
GS},
Title = {{Forces for morphogenesis investigated with laser
microsurgery and quantitative modeling}},
Journal = {{SCIENCE}},
Volume = {{300}},
Number = {{5616}},
Pages = {{145-149}},
ISSN = {{0036-8075}},
Abstract = {{We investigated the forces that connect the genetic program
of development to morphogenesis in Drosophila. We focused on
dorsal closure, a powerful model system for development and
wound healing. We found that the bulk of progress toward
closure is driven by contractility in supracellular ``purse
strings{''} and in the amnioserosa, whereas
adhesion-mediated zipping coordinates the forces produced by
the purse strings and is essential only for the end stages.
We applied quantitative modeling to show that these forces,
generated in distinct cells, are coordinated in space and
synchronized in time. Modeling of wild-type and mutant
phenotypes is predictive; although closure in myospheroid
mutants ultimately fails when the cell sheets rip themselves
apart, our analysis indicates that beta(PS) integrin has an
earlier, important role in zipping.}},
Key = {ISI:000181988900053}
}
@article{ISI:A1980KG11400938,
Author = {KIEHART, DP and POLLARD, TD},
Title = {{MONOCLONAL-ANTIBODIES TO MUSCLE MYOSIN}},
Journal = {{EUROPEAN JOURNAL OF CELL BIOLOGY}},
Volume = {{22}},
Number = {{1}},
Pages = {{317}},
ISSN = {{0171-9335}},
Key = {ISI:A1980KG11400938}
}
@article{ISI:A1995TF51301457,
Author = {AYOOB, J and KIEHART, DP and SANGER, JM and SANGER,
JW},
Title = {{MYOFIBRILLOGENESIS IN PRIMARY CULTURES OF DROSOPHILA
MYOBLASTS}},
Journal = {{MOLECULAR BIOLOGY OF THE CELL}},
Volume = {{6}},
Number = {{Suppl. S}},
Pages = {{1458}},
ISSN = {{1059-1524}},
Key = {ISI:A1995TF51301457}
}
@article{ISI:A1977DZ36000056,
Author = {KIEHART, DP and REYNOLDS, GT and EISEN, A},
Title = {{CALCIUM TRANSIENTS DURING EARLY DEVELOPMENT IN ECHINODERMS
AND TELEOSTS}},
Journal = {{BIOLOGICAL BULLETIN}},
Volume = {{153}},
Number = {{2}},
Pages = {{432}},
ISSN = {{0006-3185}},
Key = {ISI:A1977DZ36000056}
}
@article{ISI:A1983RN79500990,
Author = {KIEHART, DP and POLLARD, TD},
Title = {{MONOCLONAL-ANTIBODIES REVEAL THAT THE ACTINACTIVATED ATPASE
OF ACANTHAMOEBA MYOSIN-II IS ACTIVATED 5-10 FOLD BY ASSEMBLY
OF MYOSIN-II INTO FILAMENTS}},
Journal = {{JOURNAL OF CELL BIOLOGY}},
Volume = {{97}},
Number = {{5}},
Pages = {{A264}},
ISSN = {{0021-9525}},
Key = {ISI:A1983RN79500990}
}
@article{ISI:A1995TF51302205,
Author = {FOSS, M and LEE, BY and KIEHART, DP},
Title = {{A SCREEN FOR DROSOPHILA CELL-SHAPE DETERMINANTS THAT ALTER
S-POMBE MORPHOLOGY}},
Journal = {{MOLECULAR BIOLOGY OF THE CELL}},
Volume = {{6}},
Number = {{Suppl. S}},
Pages = {{2208}},
ISSN = {{1059-1524}},
Key = {ISI:A1995TF51302205}
}
@article{ISI:A1991HG08000897,
Author = {KIEHART, DP},
Title = {{NONMUSCLE MYOSIN IS REQUIRED FOR CELL-SHAPE CHANGE DURING
CELL SHEET MORPHOGENESIS AND CYTOKINESIS}},
Journal = {{ABSTRACTS OF PAPERS OF THE AMERICAN CHEMICAL
SOCIETY}},
Volume = {{202}},
Number = {{Part 1}},
Pages = {{140-BIOL}},
ISSN = {{0065-7727}},
Key = {ISI:A1991HG08000897}
}
@article{ISI:000088508500008,
Author = {Champagne, MB and Edwards, KA and Erickson, HP and Kiehart,
DP},
Title = {{Drosophila stretchin-MLCK is a novel member of the
Titin/Myosin light chain kinase family}},
Journal = {{JOURNAL OF MOLECULAR BIOLOGY}},
Volume = {{300}},
Number = {{4}},
Pages = {{759-777}},
ISSN = {{0022-2836}},
Abstract = {{Members of the Titin/Myosin light chain kinase family play
an essential role in the organization of the Actin/Myosin
cytoskeleton, especially in sarcomere assembly and function.
In Drosophila melanogaster, Projectin is so far the only
member of this family for which a transcription unit has
been characterized. The locus of another member of this
family, a protein related to Myosin light chain kinase, was
also identified. The cDNA and genomic sequences published
explain only the shorter transcripts expressed by this
locus. Here, we report the complete molecular
characterization of this transcription unit, which spans 38
kb, includes 33 exons and accounts for transcripts up to 25
kb in length. This transcription unit contains both the
largest exon (12,005 nt) and the largest coding region
(25,213 nt) reported so far for Drosophila. This
transcription unit features both internal promoters and
internal polyadenylation signals, which enable it to express
seven different transcripts, ranging from 3.3 to 25 kb in
size. The latter encodes a huge, Titin-Like, 926 kDa kinase
that features two large PEVK-rich repeats, 32 immunoglobulin
and two fibronectin type-III domains, which we designate
Stretchin-MLCK. In addition, the 3' end of the
Stretchin-Mlck transcription unit expresses shorter
transcripts that encode 86 to 165 kDa isoforms of
Stretchin-MLCK that are analogous to vertebrate Myosin light
chain kinases. Similarly, the 5' end of the Stretchin-Mlck
transcription unit can also express transcripts encoding
Kettin and Unc-89-like isoforms, which share no sequences
with the MLCK-like transcripts. Thus, this locus can be
viewed as a single transcription unit, Stretchin-Mlck
(genetic abbreviation Stm-Mlck), that expresses large,
composite transcripts and protein isoforms (sequences
available at http://www.academicpress.com/jmb), as well as a
complex of two independent transcription units, the
Stretchin and Mlck transcription units (Stm and Mlck,
respectively) the result of a ``gene fission{''} event, that
encode independent transcripts and proteins with distinct
structural and enzymatic functions. (C) 2000 Academic
Press.}},
Key = {ISI:000088508500008}
}
@article{ISI:000169782800052,
Author = {Kiehart, DP and Bloor, JW and Wiemann, JM and Gerald, NJ and Williams, VS and Franke, JD and Montague,
RA},
Title = {{A molecular and genetic analysis of the forces required for
morphogenesis}},
Journal = {{JOURNAL OF GENERAL PHYSIOLOGY}},
Volume = {{118}},
Number = {{1}},
Pages = {{19A}},
ISSN = {{0022-1295}},
Key = {ISI:000169782800052}
}
@article{ISI:A1986A176800523,
Author = {KIEHART, DP and FEGHALI, R},
Title = {{DROSOPHILA CYTOPLASMIC MYOSIN}},
Journal = {{BIOPHYSICAL JOURNAL}},
Volume = {{49}},
Number = {{2, Part 2}},
Pages = {{A186}},
ISSN = {{0006-3495}},
Key = {ISI:A1986A176800523}
}
@article{ISI:000076906700844,
Author = {Kiehart, DP and Galbraith, C and Montague,
RA},
Title = {{Forces for dorsal closure in Drosophila are both parallel
and perpendicular to the morphogenic movements that cause
the lateral epidermis to spread over the
amnioserosa.}},
Journal = {{MOLECULAR BIOLOGY OF THE CELL}},
Volume = {{9}},
Number = {{Suppl. S}},
Pages = {{146A}},
ISSN = {{1059-1524}},
Key = {ISI:000076906700844}
}
@article{ISI:000179569102679,
Author = {Hutson, S and Tokutake, Y and Chang, M and Bloor, JW and Venakides, S and Kiehart, DP and Edwards,
GS},
Title = {{Measuring the forces that drive morphogenesis:
Laser-microsurgery and quantitative modeling applied to
dorsal closure in Drosophila}},
Journal = {{MOLECULAR BIOLOGY OF THE CELL}},
Volume = {{13}},
Pages = {{476A}},
ISSN = {{1059-1524}},
Key = {ISI:000179569102679}
}
@article{ISI:A1991MG41700007,
Author = {KIEHART, DP},
Title = {{CONTRACTILE AND CYTOSKELETAL PROTEINS IN DROSOPHILA
EMBRYOGENESIS}},
Journal = {{CURRENT TOPICS IN MEMBRANES}},
Volume = {{38}},
Pages = {{79-97}},
Key = {ISI:A1991MG41700007}
}
@article{ISI:A1995TF51300143,
Author = {NEWBERN, EC and BAKER, J and KIEHART, DP},
Title = {{CHARACTERIZATION OF CONVENTIONAL NONMUSCLE MYOSIN-II IN
CAENORHABDITIS-ELEGANS}},
Journal = {{MOLECULAR BIOLOGY OF THE CELL}},
Volume = {{6}},
Number = {{Suppl. S}},
Pages = {{144}},
ISSN = {{1059-1524}},
Key = {ISI:A1995TF51300143}
}
@article{ISI:A1986E958902021,
Author = {BYERS, TJ and DUBREUIL, RR and KIEHART, DP and BRANTON, D and GOLDSTEIN, LSB},
Title = {{DROSOPHILA SPECTRIN}},
Journal = {{JOURNAL OF CELL BIOLOGY}},
Volume = {{103}},
Number = {{5, Part 2}},
Pages = {{A540}},
ISSN = {{0021-9525}},
Key = {ISI:A1986E958902021}
}
@article{ISI:000172372501634,
Author = {Bloor, JW and Kiehart, DP},
Title = {{RhoA function in the Drosophila epidermis}},
Journal = {{MOLECULAR BIOLOGY OF THE CELL}},
Volume = {{12}},
Number = {{Suppl. S}},
Pages = {{299A}},
ISSN = {{1059-1524}},
Key = {ISI:000172372501634}
}
@article{ISI:A1977DY90100746,
Author = {KIEHART, DP and INOUE, S and MABUCHI, I},
Title = {{EVIDENCE THAT FORCE PRODUCTION IN CHROMOSOME MOVEMENT DOES
NOT INVOLVE MYOSIN}},
Journal = {{JOURNAL OF CELL BIOLOGY}},
Volume = {{75}},
Number = {{2}},
Pages = {{A258}},
ISSN = {{0021-9525}},
Key = {ISI:A1977DY90100746}
}
@article{ISI:000077556600012,
Author = {Crawford, JM and Harden, N and Leung, T and Lim, L and Kiehart, DP},
Title = {{Cellularization in Drosophila melanogaster is disrupted by
the inhibition of Rho activity and the activation of Cdc42
function}},
Journal = {{DEVELOPMENTAL BIOLOGY}},
Volume = {{204}},
Number = {{1}},
Pages = {{151-164}},
ISSN = {{0012-1606}},
Abstract = {{Regulation of cytoskeletal dynamics is essential for cell
shape change and morphogenesis. Drosophila melanogaster
embryos offer a well-defined system for observing
alterations in the cytoskeleton during the process of
cellularization, a specialized form of cytokinesis. During
cellularization, the actomyosin cytoskeleton forms a
hexagonal array and drives invagination of the plasma
membrane between the nuclei located at the cortex of the
syncytial blastoderm. Rho, Rac, and Cdc42 proteins are
members of the Rho subfamily of Ras-related G proteins that
are involved in the formation and maintenance of the actin
cytoskeleton throughout phylogeny and in D. melanogaster. To
investigate how Rho subfamily activity affects the
cytoskeleton during cellularization stages, embryos were
microinjected with C3 exoenzyme from Clostridium botulinum
or with wild-type, constitutively active, or dominant
negative versions of Rho, Rac, and Cdc42 proteins. C3
exoenzyme ADP-ribosylates and inactivates Rho with high
specificity, whereas constitutively active dominant
mutations remain in the activated GTP-bound state to
activate downstream effecters. Dominant negative mutations
likely inhibit endogenous small G protein activity by
sequestering exchange factors. Of the 10 agents
microinjected, C3 exoenzyme, constitutively active Cdc42,
and dominant negative Rho have a specific and
indistinguishable effect: the actomyosin cytoskeleton is
disrupted, cellularization halts, and embryogenesis arrests.
Time-lapse video records of DIC imaged embryos show that
nuclei in injected regions move away from the cortex of the
embryo, thereby phenocopying injections of cytochalasin or
antimyosin. Rhodamine phalloidin staining reveals that the
actin-based hexagonal array normally seen during
cellularization is disrupted in a dose-dependent fashion.
Additionally, DNA stain reveals that nuclei in the
microinjected embryos aggregate in regions that correspond
to actin disruption. These embryos halt in cellularization
and do not proceed to gastrulation. We conclude that Rho
activity and Cdc42 regulation are required for cytoskeletal
function in actomyosin-driven furrow canal formation and
nuclear positioning. (C) 1998 Academic Press.}},
Key = {ISI:000077556600012}
}
@article{ISI:A1976BZ77400688,
Author = {KIEHART, DP and INOUE, S},
Title = {{LOCAL DEPOLYMERIZATION OF SPINDLE MICROTUBULES BY
MICROINJECTION OF CALCIUM-IONS}},
Journal = {{JOURNAL OF CELL BIOLOGY}},
Volume = {{70}},
Number = {{2}},
Pages = {{A230}},
ISSN = {{0021-9525}},
Key = {ISI:A1976BZ77400688}
}
@article{ISI:A1982NT58900003,
Author = {KIEHART, DP},
Title = {{MICRO-INJECTION OF ECHINODERM EGGS - APPARATUS AND
PROCEDURES}},
Journal = {{METHODS IN CELL BIOLOGY}},
Volume = {{25}},
Pages = {{13-31}},
ISSN = {{0091-679X}},
Key = {ISI:A1982NT58900003}
}
@article{ISI:A1975AU24800048,
Author = {MARKOWITZ, C and BESWICK, D and KIEHART, D and POWERS,
D},
Title = {{SUBUNIT INTERACTIONS OF FISH HEMOGLOBINS}},
Journal = {{BIOLOGICAL BULLETIN}},
Volume = {{149}},
Number = {{2}},
Pages = {{435-436}},
ISSN = {{0006-3185}},
Key = {ISI:A1975AU24800048}
}
@article{ISI:A1984TM94900130,
Author = {WONG, AJ and KAISER, DA and POLLARD, TD and KIEHART,
DP},
Title = {{MONOCLONAL-ANTIBODIES TO HUMAN-PLATELET MYOSIN DEMONSTRATE
CONSERVED EPITOPES AMONG HETEROLOGOUS MYOSINS}},
Journal = {{JOURNAL OF CELL BIOLOGY}},
Volume = {{99}},
Number = {{4}},
Pages = {{A36}},
ISSN = {{0021-9525}},
Key = {ISI:A1984TM94900130}
}
%% Edited Volumes
@article{fds52167,
Author = {D.P. Kiehart and K. Bloom},
Title = {Cell Structure and Dynamics},
Journal = {Current Opinion in Cell Biology},
Volume = {19},
Number = {1},
Pages = {1-108},
Year = {2007},
Month = {February},
Key = {fds52167}
}
%% Published Abstracts
@article{fds143526,
Author = {Singh, V. and J.D.Franke, M. Chee and D.P. Kiehart},
Title = {Investigating the role of crinkled (ck) Myosin VIIA in the
morphogenesis of actin-rich cellular projections in
Drosophila melanogaster},
Journal = {Drosophila Research Conferences},
Year = {2007},
Month = {March},
Key = {fds143526}
}
@article{fds143524,
Author = {Rodriguez-Diaz, A. and D.L. Abravanel and G.S. Edwards and D.P.
Kiehart},
Title = {The contribution of the contractile actomyosin purse-string
to dorsal closure during Drosophila morphogenesis
investigated by UV laser microsurgery.},
Journal = {Biophysical Journal},
Year = {2007},
Month = {March},
Key = {fds143524}
}
@article{fds143525,
Author = {Wells, A.R. and D.P. Kiehart},
Title = {Quantitative analysis of morphogenesis during the transition
of Drosophila embryos to dorsal closure},
Journal = {Biophysical Journal},
Year = {2007},
Month = {March},
Key = {fds143525}
}
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