Source:http://linkedlifedata.com/resource/pubmed/id/10846184
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
34
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pubmed:dateCreated |
2000-9-25
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pubmed:abstractText |
Src-mediated tyrosine phosphorylation of N-methyl-d-aspartate receptor subunits has been shown to modify the functional properties of N-methyl-d-aspartate receptors. Moreover, calpain-mediated truncation of N-methyl-d-aspartate receptor subunits has been found to alter the structure of the receptors. In the present study, we first used immunoprecipitation with a variety of antibodies against N-methyl-d-aspartate receptor subunits and anti-phosphotyrosine antibodies to show that tyrosine-phosphorylated subunits of N-methyl-d-aspartate receptor are protected against calpain-mediated truncation of their C-terminal domains. A GST fusion protein containing the C-terminal domain of NR2A was used to identify the calpain cutting sites in the C-terminal domain. One site was identified at residues 1278-1279, corresponding to one of the preferred calpain truncation sites. This site is adjacent to a consensus sequence for Src-mediated tyrosine phosphorylation, and Src-mediated tyrosine phosphorylation of the GST-NR2A C-terminal fusion protein also inhibited calpain-mediated truncation of the fusion protein. We propose that phosphorylation of NR2 subunits and the resulting inhibition of calpain-mediated truncation of their C-terminal domains provide for the stabilization of the N-methyl-d-aspartate receptors in postsynaptic structures.
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pubmed:grant | |
pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Calpain,
http://linkedlifedata.com/resource/pubmed/chemical/NR2A NMDA receptor,
http://linkedlifedata.com/resource/pubmed/chemical/NR2B NMDA receptor,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, N-Methyl-D-Aspartate,
http://linkedlifedata.com/resource/pubmed/chemical/Tyrosine
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pubmed:status |
MEDLINE
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pubmed:month |
Aug
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pubmed:issn |
0021-9258
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
25
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pubmed:volume |
275
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
26477-83
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pubmed:dateRevised |
2007-11-14
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pubmed:meshHeading |
pubmed-meshheading:10846184-Amino Acid Sequence,
pubmed-meshheading:10846184-Animals,
pubmed-meshheading:10846184-Blotting, Western,
pubmed-meshheading:10846184-Calpain,
pubmed-meshheading:10846184-Gene Library,
pubmed-meshheading:10846184-Molecular Sequence Data,
pubmed-meshheading:10846184-Phosphorylation,
pubmed-meshheading:10846184-Rats,
pubmed-meshheading:10846184-Rats, Sprague-Dawley,
pubmed-meshheading:10846184-Receptors, N-Methyl-D-Aspartate,
pubmed-meshheading:10846184-Synaptic Membranes,
pubmed-meshheading:10846184-Tyrosine,
pubmed-meshheading:10846184-src Homology Domains
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pubmed:year |
2000
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pubmed:articleTitle |
Src-mediated tyrosine phosphorylation of NR2 subunits of N-methyl-D-aspartate receptors protects from calpain-mediated truncation of their C-terminal domains.
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pubmed:affiliation |
Neuroscience Program, University of Southern California, Los Angeles, California 90089-2520, 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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