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
Science. 2001 293 (5533): 1317-20

PMID: 11509731 · DOI:10.1126/science.1061086

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.

MeSH Terms (28)

Amino Acid Sequence Amino Acid Substitution Animals Biological Transport Calcium-Calmodulin-Dependent Protein Kinases Calcium-Calmodulin-Dependent Protein Kinase Type 2 Calmodulin-Binding Proteins Cell Extracts Egtazic Acid Enzyme Inhibitors Interphase Mass Spectrometry Melanophores Melanosomes Mitosis Molecular Motor Proteins Molecular Sequence Data Mutation Myosin Type V Nerve Tissue Proteins Ovum Peptides Phosphopeptides Phosphorylation Phosphoserine Recombinant Fusion Proteins Transfection Xenopus

Connections (1)

This publication is referenced by other Labnodes entities:

Links