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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
5
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pubmed:dateCreated |
2004-9-7
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pubmed:abstractText |
WNK (with no lysine [K]) protein kinases were named for their unique active site organization. Mutations in WNK1 and WNK4 cause a familial form of hypertension by undefined mechanisms. Here, we report that WNK1 selectively binds to and phosphorylates synaptotagmin 2 (Syt2) within its calcium binding C2 domains. Endogenous WNK1 and Syt2 coimmunoprecipitate and colocalize on a subset of secretory granules in INS-1 cells. Phosphorylation by WNK1 increases the amount of Ca2+ required for Syt2 binding to phospholipid vesicles; mutation of threonine 202, a WNK1 phosphorylation site, partially prevents this change. These findings suggest that phosphorylation of Syts by WNK1 can regulate Ca2+ sensing and the subsequent Ca2+-dependent interactions mediated by Syt C2 domains. These findings provide a biochemical mechanism that could lead to the retention or insertion of proteins in the plasma membrane. Interruption of this regulatory pathway may disturb membrane events that regulate ion balance.
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pubmed:grant |
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:month |
Sep
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pubmed:issn |
1097-2765
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pubmed:author |
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pubmed:copyrightInfo |
Copyright 2004 Cell Press
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pubmed:issnType |
Print
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pubmed:day |
10
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pubmed:volume |
15
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
741-51
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pubmed:dateRevised |
2011-11-17
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pubmed:meshHeading |
pubmed-meshheading:15350218-Animals,
pubmed-meshheading:15350218-Binding Sites,
pubmed-meshheading:15350218-Calcium Signaling,
pubmed-meshheading:15350218-Calcium-Binding Proteins,
pubmed-meshheading:15350218-Cell Line,
pubmed-meshheading:15350218-Cell Membrane,
pubmed-meshheading:15350218-Humans,
pubmed-meshheading:15350218-Intracellular Signaling Peptides and Proteins,
pubmed-meshheading:15350218-Mutation,
pubmed-meshheading:15350218-Nerve Tissue Proteins,
pubmed-meshheading:15350218-Phosphorylation,
pubmed-meshheading:15350218-Protein Binding,
pubmed-meshheading:15350218-Protein Structure, Tertiary,
pubmed-meshheading:15350218-Protein-Serine-Threonine Kinases,
pubmed-meshheading:15350218-Secretory Vesicles,
pubmed-meshheading:15350218-Synaptotagmin II,
pubmed-meshheading:15350218-Threonine,
pubmed-meshheading:15350218-Two-Hybrid System Techniques,
pubmed-meshheading:15350218-Water-Electrolyte Balance
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pubmed:year |
2004
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pubmed:articleTitle |
WNK1 phosphorylates synaptotagmin 2 and modulates its membrane binding.
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pubmed:affiliation |
Department of Pharmacology, The University of Texas Southwestern Medical Center, 5323 Harry Hines Boulevard, Dallas, TX 75390, USA.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, Non-U.S. Gov't
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