Fitzpatrick Institute for Photonics Fitzpatrick Institute for Photonics
Pratt School of Engineering
Duke University

 HOME > pratt > FIP    Search Help Login pdf version printable version 

Publications [#113115] of Harold P. Erickson

Papers Published

  1. J Kumar, HP Erickson, MP Sheetz, Ultrastructural and biochemical properties of the 120-kDa form of chick kinectin., The Journal of biological chemistry, UNITED STATES, vol. 273 no. 48 (November, 1998), pp. 31738-43, ISSN 0021-9258
    (last updated on 2009/02/12)

    Abstract:
    Kinectin, an integral membrane protein (160 kDa), was identified as a kinesin-binding protein. Analysis of the predicted amino acid sequence of kinectin cDNA indicated an alpha-helical coiled-coil structure from amino acid 320 to 1310. A 120-kDa kinectin has been observed consistently, and N-terminal sequencing showed that 232 amino acids were missing from the N terminus of full-length kinectin. 120-kDa kinectin was distributed in the supernatant and a low density fraction of vesicles, whereas both forms were in the high density fraction of vesicles. In the electron microscope, the 120-kDa form appeared as a linear molecule of 133 nm in length. In hydrodynamic studies, the cytosolic 120-kDa kinectin was a dimer. Monoclonal antibody molecules (anti-kinectin KR160.9) bound asymmetrically to kinectin often with two antibodies/kinectin, indicative of a parallel coiled-coil. Metabolic labeling with [3H]myristic acid showed that both the 120- and 160-kDa kinectin are myristoylated in chick embryo fibroblasts. The myristoylation of 120-kDa kinectin may provide a mechanism for linking it to a low density fraction of vesicles. Immunoprecipitation with a 160-kDa kinectin-specific antibody brought down the 120-kDa kinectin. Thus, we suggest that kinectin is an extended parallel coiled-coil dimer, often a heterodimer.

    Keywords:
    Amino Acid Sequence • Animals • Antibodies, Monoclonal • Binding Sites, Antibody • Cells, Cultured • Chick Embryo • Chickens • DNA, Complementary • Membrane Proteins* • Microscopy, Electron • Molecular Sequence Data • Molecular Weight • Myristic Acid • Protein Conformation • RNA, Messenger • Receptors, Cell Surface • chemistry* • genetics • metabolism • ultrastructure*


Duke University * Pratt * Reload * Login