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Ultrastructural and biochemical properties of the 120-kDa form of chick kinectin.

Publication ,  Journal Article
Kumar, J; Erickson, HP; Sheetz, MP
Published in: J Biol Chem
November 27, 1998

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.

Duke Scholars

Published In

J Biol Chem

DOI

ISSN

0021-9258

Publication Date

November 27, 1998

Volume

273

Issue

48

Start / End Page

31738 / 31743

Location

United States

Related Subject Headings

  • Receptors, Cell Surface
  • RNA, Messenger
  • Protein Conformation
  • Myristic Acid
  • Molecular Weight
  • Molecular Sequence Data
  • Microscopy, Electron
  • Membrane Proteins
  • DNA, Complementary
  • Chickens
 

Citation

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Kumar, J., Erickson, H. P., & Sheetz, M. P. (1998). Ultrastructural and biochemical properties of the 120-kDa form of chick kinectin. J Biol Chem, 273(48), 31738–31743. https://doi.org/10.1074/jbc.273.48.31738
Kumar, J., H. P. Erickson, and M. P. Sheetz. “Ultrastructural and biochemical properties of the 120-kDa form of chick kinectin.J Biol Chem 273, no. 48 (November 27, 1998): 31738–43. https://doi.org/10.1074/jbc.273.48.31738.
Kumar J, Erickson HP, Sheetz MP. Ultrastructural and biochemical properties of the 120-kDa form of chick kinectin. J Biol Chem. 1998 Nov 27;273(48):31738–43.
Kumar, J., et al. “Ultrastructural and biochemical properties of the 120-kDa form of chick kinectin.J Biol Chem, vol. 273, no. 48, Nov. 1998, pp. 31738–43. Pubmed, doi:10.1074/jbc.273.48.31738.
Kumar J, Erickson HP, Sheetz MP. Ultrastructural and biochemical properties of the 120-kDa form of chick kinectin. J Biol Chem. 1998 Nov 27;273(48):31738–31743.

Published In

J Biol Chem

DOI

ISSN

0021-9258

Publication Date

November 27, 1998

Volume

273

Issue

48

Start / End Page

31738 / 31743

Location

United States

Related Subject Headings

  • Receptors, Cell Surface
  • RNA, Messenger
  • Protein Conformation
  • Myristic Acid
  • Molecular Weight
  • Molecular Sequence Data
  • Microscopy, Electron
  • Membrane Proteins
  • DNA, Complementary
  • Chickens