title: Cell cycle regulation of myosin-V by calcium/calmodulin-dependent protein kinase II.
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.
authors.affiliation: Department of Cell and Structural Biology, University of Illinois at Urbana-Champaign, Urbana, IL 61801, USA.
authors.forename: R L
authors.initials: RL
authors.lastname: Karcher
authors.forename: J T
authors.initials: JT
authors.lastname: Roland
authors.forename: F
authors.initials: F
authors.lastname: Zappacosta
authors.forename: M J
authors.initials: MJ
authors.lastname: Huddleston
authors.forename: R S
authors.initials: RS
authors.lastname: Annan
authors.forename: S A
authors.initials: SA
authors.lastname: Carr
authors.forename: V I
authors.initials: VI
authors.lastname: Gelfand
mesh_terms: D000595:Amino Acid Sequence; D019943:Amino Acid Substitution; D000818:Animals; D001692:Biological Transport; D054732:Calcium-Calmodulin-Dependent Protein Kinase Type 2; D017871:Calcium-Calmodulin-Dependent Protein Kinases / Q000037:antagonists & inhibitors / Q000378:metabolism*; D002148:Calmodulin-Binding Proteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D002457:Cell Extracts; D004533:Egtazic Acid / Q000031:analogs & derivatives / Q000494:pharmacology; D004791:Enzyme Inhibitors / Q000494:pharmacology; D007399:Interphase; D013058:Mass Spectrometry; D008547:Melanophores / Q000378:metabolism / Q000648:ultrastructure; D020460:Melanosomes / Q000378:metabolism*; D008938:Mitosis; D020409:Molecular Motor Proteins / Q000378:metabolism*; D008969:Molecular Sequence Data; D009154:Mutation; D024701:Myosin Type V; D009419:Nerve Tissue Proteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D010063:Ovum; D010455:Peptides / Q000494:pharmacology; D010748:Phosphopeptides / Q000032:analysis / Q000378:metabolism; D010766:Phosphorylation; D010768:Phosphoserine / Q000378:metabolism; D011993:Recombinant Fusion Proteins / Q000378:metabolism; D014162:Transfection; D014981:Xenopus
chemical_list: D002148:Calmodulin-Binding Proteins; D002457:Cell Extracts; D004791:Enzyme Inhibitors; D020409:Molecular Motor Proteins; D009419:Nerve Tissue Proteins; D010455:Peptides; D010748:Phosphopeptides; D011993:Recombinant Fusion Proteins; C078829:chicken brain myosin-V p190; D010768:Phosphoserine; D004533:Egtazic Acid; D054732:Calcium-Calmodulin-Dependent Protein Kinase Type 2; D017871:Calcium-Calmodulin-Dependent Protein Kinases; D024701:Myosin Type V; C025603:1,2-bis(2-aminophenoxy)ethane-N,N,N',N'-tetraacetic acid