Phosphotransferases associated with the regulation of kinesin motor activity

J Biol Chem. 1997 Sep 5;272(36):22929-33. doi: 10.1074/jbc.272.36.22929.

Abstract

Kinesin, a plus-end-directed microtubule motor protein, functions in concert with accessory factors that have been shown to regulate enzyme activity and may also provide cargo specificity. This report identifies teh 79-kDa kinesin-associated phosphoprotein as a phosphoisoform of kinesin light chain. Increased phosphorylation of this light chain isoform is sufficient to account for the increase in kinesin-mediated microtubule-gliding activity. Additionally, it was found that the degree of phosphorylation of this isoform is regulated by a 100-kDa kinase and 150-kDa type 1 phosphatase. Both the kinesin light chain kinase and phosphatase co-purify with the kinesin heavy chain, suggesting that kinesin exists in a large complex capable of self-regulation.

Publication types

  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Animals
  • Cell Line
  • Chick Embryo
  • Kinesins / metabolism*
  • Mice
  • Phosphorylation
  • Phosphotransferases / metabolism*

Substances

  • Phosphotransferases
  • Kinesins