Publications [#112810] of G Vann V. Bennett

Papers Published

1. Y Matsuoka, CA Hughes, V Bennett, Adducin regulation. Definition of the calmodulin-binding domain and sites of phosphorylation by protein kinases A and C., The Journal of biological chemistry, UNITED STATES, vol. 271 no. 41 (October, 1996), pp. 25157-66, ISSN 0021-9258
   (last updated on 2003/02/18)

   Abstract:
   Adducin promotes association of spectrin with actin and caps the fast growing end of actin filaments. Adducin contains N-terminal core, neck, and C-terminal tail domains, is a substrate for protein kinases A (PKA) and C (PKC), and binds to Ca2+/calmodulin. Ser-726 and Ser-713 in the C-terminal MARCKS-related domains of alpha- and beta-adducin, respectively, were identified as the major phosphorylation sites common for PKA and PKC. PKA, in addition, phosphorylated alpha-adducin at Ser-408, -436, and -481 in the neck domain. Phosphorylation by PKA, but not PKC, reduced the affinity of adducin for spectrin-F-actin complexes as well as the activity of adducin in promoting binding of spectrin to F-actin. The myristoylated alanine-rich protein kinase C substrate-related domain of beta-adducin was identified as the dominant Ca2+-dependent calmodulin-binding site. Calmodulin-binding was inhibited by phosphorylation of beta-adducin and of a MARCKS-related domain peptide by PKA and PKC. Calmodulin in turn inhibited the rate, but not the extent, of phosphorylation of beta-adducin, but not alpha-adducin, by PKA and that of each subunit by PKC. These findings suggest a complex reciprocal relationship between regulation of adducin function by calmodulin binding and phosphorylation by PKA and PKC.

   Keywords:
   Amino Acid Sequence • Binding Sites • Calmodulin • Calmodulin-Binding Proteins • Chromatography, High Pressure Liquid • Cyclic AMP-Dependent Protein Kinases • Cytoskeletal Proteins • Erythrocytes • Humans • Intracellular Signaling Peptides and Proteins* • Kinetics • Membrane Proteins* • Molecular Sequence Data • Peptide Fragments • Phosphopeptides • Phosphorylation • Phosphoserine • Phosphothreonine • Phosphotyrosine • Protein Kinase C • Proteins • analysis • chemical synthesis • chemistry • isolation & purification • metabolism • metabolism*