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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
6615
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pubmed:dateCreated |
1997-2-12
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pubmed:abstractText |
The mechanisms by which neurotransmitter receptors are immobilized at postsynaptic sites in neurons are largely unknown. The activity of NMDA (N-methyl-D-aspartate) receptors is mechanosensitive and dependent on the integrity of actin, suggesting a functionally important interaction between NMDA receptors and the postsynaptic cytoskeleton. alpha-Actinin-2, a member of the spectrin/dystrophin family of actin-binding proteins, is identified here as a brain postsynaptic density protein that colocalizes in dendritic spines with NMDA receptors and the putative NMDA receptor-clustering molecule PSD-95. alpha-Actinin-2 binds by its central rod domain to the cytoplasmic tail of both NR1 and NR2B subunits of the NMDA receptor, and can be immunoprecipitated with NMDA receptors and PSD-95 from rat brain. Intriguingly, NR1-alpha-actinin binding is directly antagonized by Ca2+/calmodulin. Thus alpha-actinin may play a role in both the localization of NMDA receptors and their modulation by Ca2+.
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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/Actins,
http://linkedlifedata.com/resource/pubmed/chemical/Calmodulin,
http://linkedlifedata.com/resource/pubmed/chemical/Dlgh4 protein, rat,
http://linkedlifedata.com/resource/pubmed/chemical/Intracellular Signaling Peptides...,
http://linkedlifedata.com/resource/pubmed/chemical/KCNA4 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Kcna4 protein, rat,
http://linkedlifedata.com/resource/pubmed/chemical/Kv1.4 Potassium Channel,
http://linkedlifedata.com/resource/pubmed/chemical/Membrane Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Nerve Tissue Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Potassium Channels,
http://linkedlifedata.com/resource/pubmed/chemical/Potassium Channels, Voltage-Gated,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, N-Methyl-D-Aspartate,
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Fusion Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/postsynaptic density proteins
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pubmed:status |
MEDLINE
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pubmed:month |
Jan
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pubmed:issn |
0028-0836
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
30
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pubmed:volume |
385
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
439-42
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:9009191-Actins,
pubmed-meshheading:9009191-Amino Acid Sequence,
pubmed-meshheading:9009191-Animals,
pubmed-meshheading:9009191-Binding, Competitive,
pubmed-meshheading:9009191-Binding Sites,
pubmed-meshheading:9009191-Brain,
pubmed-meshheading:9009191-Calmodulin,
pubmed-meshheading:9009191-Cells, Cultured,
pubmed-meshheading:9009191-Hippocampus,
pubmed-meshheading:9009191-Humans,
pubmed-meshheading:9009191-Intracellular Signaling Peptides and Proteins,
pubmed-meshheading:9009191-Kv1.4 Potassium Channel,
pubmed-meshheading:9009191-Membrane Proteins,
pubmed-meshheading:9009191-Molecular Sequence Data,
pubmed-meshheading:9009191-Nerve Tissue Proteins,
pubmed-meshheading:9009191-Neurons,
pubmed-meshheading:9009191-Potassium Channels,
pubmed-meshheading:9009191-Potassium Channels, Voltage-Gated,
pubmed-meshheading:9009191-Rats,
pubmed-meshheading:9009191-Receptors, N-Methyl-D-Aspartate,
pubmed-meshheading:9009191-Recombinant Fusion Proteins
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pubmed:year |
1997
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pubmed:articleTitle |
Competitive binding of alpha-actinin and calmodulin to the NMDA receptor.
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pubmed:affiliation |
Howard Hughes Medical Institute, Harvard Medical School, Boston, Massachusetts 02114, 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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