Cell cycle regulation of myosin-V by calcium/calmodulin - Dependent protein kinase II

R. L. Karcher, J. T. Roland, F. Zappacosta, M. J. Huddleston, R. S. Annan, S. A. Carr, V. I. Gelfand*

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

118 Scopus citations

Abstract

Organelle transport by myosin-V is down-regulated during mitosis, presumably by myosin-V phosphorylation. We used mass spectrometry phosphopeptide mapping to show that the tail of myosin-V was phosphorylated in mitotic Xenopus egg extract on a single serine residue localized in the carboxyl-terminal organelle-binding domain. Phosphorylation resulted in the release of the motor from the organelle. The phosphorylation site matched the consensus sequence of calcium/calmodulin-dependent protein kinase II (CaMKII), and inhibitors of CaMKII prevented myosin-V release. The modulation of cargo binding by phosphorylation is likely to represent a general mechanism regulating organelle transport by myosin-V.

Original languageEnglish (US)
Pages (from-to)1317-1320
Number of pages4
JournalScience
Volume293
Issue number5533
DOIs
StatePublished - Aug 17 2001

ASJC Scopus subject areas

  • General

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