Regulation of kinesin activity by phosphorylation of kinesin-associated proteins

James M. McIlvain, Janis K. Burkhardt, Sarah Hamm-Alvarez, Yair Argon, Michael Sheetz

Research output: Contribution to journalArticle

72 Citations (Scopus)

Abstract

The mechanochemical motor proteins of the kinesin and cytoplasmic dynein families play important roles in microtubule-based intracellular motility. Although movement and distribution of organelles like secretory granules, vesicles, endoplasmic reticulum, and chromosomes depend on the activity of these motor proteins, little is known about the regulation of this movement. We report here that the hyperphosphorylation of components of the kinesin complex by treatment with okadaic acid increases kinesin motor activity at least 2-fold. The stimulation was observed using both a granule motility assay and a microtubule gliding assay, indicating that phosphorylation enhances the activity of the motor itself, rather than the affinity of the motor for membrane organelles. Under stimulatory conditions, three proteins that co-purify with kinesin (with mobilities of 150, 79, and 73 kDa) are consistently hyperphosphorylated. Dephosphorylation of these proteins reduces kinesin activity to basal levels. Therefore, we conclude that kinesin motor activity is directly modulated by the phosphorylation state of kinesin- associated proteins.

Original languageEnglish (US)
Pages (from-to)19176-19182
Number of pages7
JournalJournal of Biological Chemistry
Volume269
Issue number29
StatePublished - Jul 22 1994
Externally publishedYes

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Kinesin
Phosphorylation
Motor Activity
Proteins
Secretory Vesicles
Microtubules
Organelles
Assays
Cytoplasmic Dyneins
Okadaic Acid
Chromosomes
Endoplasmic Reticulum
Membranes

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology
  • Cell Biology

Cite this

McIlvain, J. M., Burkhardt, J. K., Hamm-Alvarez, S., Argon, Y., & Sheetz, M. (1994). Regulation of kinesin activity by phosphorylation of kinesin-associated proteins. Journal of Biological Chemistry, 269(29), 19176-19182.

Regulation of kinesin activity by phosphorylation of kinesin-associated proteins. / McIlvain, James M.; Burkhardt, Janis K.; Hamm-Alvarez, Sarah; Argon, Yair; Sheetz, Michael.

In: Journal of Biological Chemistry, Vol. 269, No. 29, 22.07.1994, p. 19176-19182.

Research output: Contribution to journalArticle

McIlvain, JM, Burkhardt, JK, Hamm-Alvarez, S, Argon, Y & Sheetz, M 1994, 'Regulation of kinesin activity by phosphorylation of kinesin-associated proteins', Journal of Biological Chemistry, vol. 269, no. 29, pp. 19176-19182.
McIlvain JM, Burkhardt JK, Hamm-Alvarez S, Argon Y, Sheetz M. Regulation of kinesin activity by phosphorylation of kinesin-associated proteins. Journal of Biological Chemistry. 1994 Jul 22;269(29):19176-19182.
McIlvain, James M. ; Burkhardt, Janis K. ; Hamm-Alvarez, Sarah ; Argon, Yair ; Sheetz, Michael. / Regulation of kinesin activity by phosphorylation of kinesin-associated proteins. In: Journal of Biological Chemistry. 1994 ; Vol. 269, No. 29. pp. 19176-19182.
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