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XB-ART-8548
Science 2001 Aug 17;2935533:1317-20. doi: 10.1126/science.1061086.
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Cell cycle regulation of myosin-V by calcium/calmodulin-dependent protein kinase II.

Karcher RL , Roland JT , Zappacosta F , Huddleston MJ , Annan RS , Carr SA , Gelfand VI .


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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.

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Species referenced: Xenopus
Genes referenced: camk2g

References :
Cheney, Cell biology. A switch to release the motor. 2001, Pubmed, Xenbase