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Cell Cycle Regulation of Myosin-V by Calcium/Calmodulin-Dependent Protein Kinase II

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Science  17 Aug 2001:
Vol. 293, Issue 5533, pp. 1317-1320
DOI: 10.1126/science.1061086

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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.

  • * Present address: Millennium Pharmaceuticals, Cambridge, MA 02139, USA.

  • To whom correspondence should be addressed. E-mail: vgelfand{at}life.uiuc.edu

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