Report

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

See allHide authors and affiliations

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

You are currently viewing the abstract.

View Full Text

Log in to view the full text

Log in through your institution

Log in through your institution

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

View Full Text