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Science 17 August 2001:
Vol. 293. no. 5533, pp. 1317 - 1320
DOI: 10.1126/science.1061086
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Reports

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

Ryan L. Karcher,1 Joseph T. Roland,1 Francesca Zappacosta,2 Michael J. Huddleston,2 Roland S. Annan,2 Steven A. Carr,2* Vladimir I. Gelfand1dagger

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.

1 Department of Cell and Structural Biology, University of Illinois at Urbana-Champaign, Urbana, IL 61801, USA.
2 Department of Physical and Structural Chemistry, GlaxoSmithKline, King of Prussia, PA 19406, USA.
*   Present address: Millennium Pharmaceuticals, Cambridge, MA 02139, USA.

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

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