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PMID: 9312551 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, P.H.S.

Phosphotransferases associated with the regulation of kinesin motor activity.

The Journal of biological chemistry ·Vol. 272 ·No. 36 ·1997-09-05 ·Pages 22929-33

Lindesmith L, McIlvain JM, Argon Y, Sheetz MP

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.

MeSH Terms
Animals Cell Line Chick Embryo Kinesins/metabolism Mice Phosphorylation Phosphotransferases/metabolism
Chemicals
Phosphotransferases Kinesins
Authors & Affiliations
4 authors, click to expand affiliations / ORCID
Lindesmith L
Department of Cell Biology, Duke University Medical Center, Durham, North Carolina 27710, USA.
McIlvain J M
Argon Y
Sheetz M P
Article Info
Journal
The Journal of biological chemistry
Abbr.
J Biol Chem
ISSN
0021-9258
Published
1997-09-05
Pages
22929-33
Language
English
Region
United States
NLM ID
2985121R
Subset
IM
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