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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
49
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pubmed:dateCreated |
2004-11-25
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pubmed:abstractText |
TRPM7 is an unusual bifunctional molecule consisting of a TRP ion channel fused to a protein kinase domain. It has been shown that TRPM7 plays a key role in the regulation of intracellular magnesium homeostasis as well as in anoxic neuronal death. TRPM7 channel has been characterized using electrophysiological techniques; however, the function of the kinase domain is not known and endogenous substrates for the kinase have not been reported previously. Here we have identified annexin 1 as a substrate for TRPM7 kinase. Phosphorylation of annexin 1 by TRPM7 kinase is stimulated by Ca2+ and is dramatically increased in extracts from cells overexpressing TRPM7. Phosphorylation of annexin 1 by TRPM7 kinase occurs at a conserved serine residue (Ser5) located within the N-terminal amphipathic alpha-helix of annexin 1. The N-terminal region plays a crucial role in interaction of annexin 1 with other proteins and membranes, and therefore, phosphorylation of annexin 1 at Ser5 by TRPM7 kinase may modulate function of annexin 1.
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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 |
http://linkedlifedata.com/resource/pubmed/chemical/Annexin A1,
http://linkedlifedata.com/resource/pubmed/chemical/Calcium,
http://linkedlifedata.com/resource/pubmed/chemical/Cathepsin D,
http://linkedlifedata.com/resource/pubmed/chemical/Ion Channels,
http://linkedlifedata.com/resource/pubmed/chemical/Ions,
http://linkedlifedata.com/resource/pubmed/chemical/Magnesium,
http://linkedlifedata.com/resource/pubmed/chemical/Membrane Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Peptides,
http://linkedlifedata.com/resource/pubmed/chemical/Protein Kinases,
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Serine,
http://linkedlifedata.com/resource/pubmed/chemical/TRPM Cation Channels,
http://linkedlifedata.com/resource/pubmed/chemical/Trpm7 protein, mouse,
http://linkedlifedata.com/resource/pubmed/chemical/Trypsin
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pubmed:status |
MEDLINE
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pubmed:month |
Dec
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pubmed:issn |
0021-9258
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
3
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pubmed:volume |
279
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
50643-6
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pubmed:dateRevised |
2009-11-19
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pubmed:meshHeading |
pubmed-meshheading:15485879-Amino Acid Sequence,
pubmed-meshheading:15485879-Animals,
pubmed-meshheading:15485879-Annexin A1,
pubmed-meshheading:15485879-Binding Sites,
pubmed-meshheading:15485879-Calcium,
pubmed-meshheading:15485879-Cathepsin D,
pubmed-meshheading:15485879-Cell Line,
pubmed-meshheading:15485879-Electrophoresis, Gel, Two-Dimensional,
pubmed-meshheading:15485879-Electrophoresis, Polyacrylamide Gel,
pubmed-meshheading:15485879-Humans,
pubmed-meshheading:15485879-Ion Channels,
pubmed-meshheading:15485879-Ions,
pubmed-meshheading:15485879-Magnesium,
pubmed-meshheading:15485879-Membrane Proteins,
pubmed-meshheading:15485879-Mice,
pubmed-meshheading:15485879-Models, Molecular,
pubmed-meshheading:15485879-Molecular Sequence Data,
pubmed-meshheading:15485879-Mutagenesis, Site-Directed,
pubmed-meshheading:15485879-Peptides,
pubmed-meshheading:15485879-Phosphorylation,
pubmed-meshheading:15485879-Polymerase Chain Reaction,
pubmed-meshheading:15485879-Protein Binding,
pubmed-meshheading:15485879-Protein Kinases,
pubmed-meshheading:15485879-Protein Structure, Tertiary,
pubmed-meshheading:15485879-Recombinant Proteins,
pubmed-meshheading:15485879-Sequence Homology, Amino Acid,
pubmed-meshheading:15485879-Serine,
pubmed-meshheading:15485879-Spectrometry, Mass, Matrix-Assisted Laser...,
pubmed-meshheading:15485879-TRPM Cation Channels,
pubmed-meshheading:15485879-Trypsin
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pubmed:year |
2004
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pubmed:articleTitle |
Phosphorylation of annexin I by TRPM7 channel-kinase.
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pubmed:affiliation |
Department of Pharmacology, University of Medicine and Dentistry of New Jersey, Robert Wood Johnson Medical School, Piscataway, New Jersey 08854, USA.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.
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