Publication Date:
2001-08-18
Description:
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.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Karcher, R L -- Roland, J T -- Zappacosta, F -- Huddleston, M J -- Annan, R S -- Carr, S A -- Gelfand, V I -- GM-52111/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 2001 Aug 17;293(5533):1317-20.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Cell and Structural Biology, University of Illinois at Urbana-Champaign, Urbana, IL 61801, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11509731" target="_blank"〉PubMed〈/a〉
Keywords:
Amino Acid Sequence
;
Amino Acid Substitution
;
Animals
;
Biological Transport
;
Calcium-Calmodulin-Dependent Protein Kinase Type 2
;
Calcium-Calmodulin-Dependent Protein Kinases/antagonists & inhibitors/*metabolism
;
Calmodulin-Binding Proteins/chemistry/genetics/*metabolism
;
Cell Extracts
;
Egtazic Acid/analogs & derivatives/pharmacology
;
Enzyme Inhibitors/pharmacology
;
Interphase
;
Mass Spectrometry
;
Melanophores/metabolism/ultrastructure
;
Melanosomes/*metabolism
;
*Mitosis
;
Molecular Motor Proteins/*metabolism
;
Molecular Sequence Data
;
Mutation
;
*Myosin Type V
;
Nerve Tissue Proteins/chemistry/genetics/*metabolism
;
Ovum
;
Peptides/pharmacology
;
Phosphopeptides/analysis/metabolism
;
Phosphorylation
;
Phosphoserine/metabolism
;
Recombinant Fusion Proteins/metabolism
;
Transfection
;
Xenopus
Print ISSN:
0036-8075
Electronic ISSN:
1095-9203
Topics:
Biology
,
Chemistry and Pharmacology
,
Computer Science
,
Medicine
,
Natural Sciences in General
,
Physics
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