Phosphotransferases associated with the regulation of kinesin motor activity

Lisa Lindesmith, James M. McIlvain, Yair Argon, Michael P. Sheetz

Research output: Contribution to journalArticlepeer-review

37 Scopus citations

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 the 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.

Original languageEnglish (US)
Pages (from-to)22929-22933
Number of pages5
JournalJournal of Biological Chemistry
Volume272
Issue number36
DOIs
StatePublished - Sep 5 1997
Externally publishedYes

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology
  • Cell Biology

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