Competitive binding of α-actinin and calmodulin to the NMDA receptor
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 1 and dependent on the integrity of actin 2 , suggesting a functionally important interaction between N...
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| Veröffentlicht in: | Nature (London) 1997-01, Vol.385 (6615), p.439-442 |
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| creator | Wyszynski, Michael Lin, Jerry Rao, Anuradha Nigh, Elizabeth Beggs, Alan H Craig, Ann Marie Sheng, Morgan |
| description | 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
1
and dependent on the integrity of actin
2
, suggesting a functionally important interaction between NMDA receptors and the postsynaptic cytoskeleton. α-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. α-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-α-actinin binding is directly antagonized by Ca
2+
/calmodulin. Thus α-actinin may play a role in both the localization of NMDA receptors and their modulation by Ca
2+
. |
| doi_str_mv | 10.1038/385439a0 |
| format | Article |
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N
-methyl-D-aspartate) receptors is mechanosensitive
1
and dependent on the integrity of actin
2
, suggesting a functionally important interaction between NMDA receptors and the postsynaptic cytoskeleton. α-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. α-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-α-actinin binding is directly antagonized by Ca
2+
/calmodulin. Thus α-actinin may play a role in both the localization of NMDA receptors and their modulation by Ca
2+
.</description><identifier>ISSN: 0028-0836</identifier><identifier>EISSN: 1476-4687</identifier><identifier>DOI: 10.1038/385439a0</identifier><identifier>PMID: 9009191</identifier><identifier>CODEN: NATUAS</identifier><language>eng</language><publisher>London: Nature Publishing Group UK</publisher><subject>Actins - metabolism ; Amino Acid Sequence ; Aminoacid receptors (glycine, glutamate, gaba) ; Animals ; Binding Sites ; Binding, Competitive ; Biological and medical sciences ; Brain ; Brain - metabolism ; Calmodulin - metabolism ; Cell receptors ; Cell structures and functions ; Cells, Cultured ; Cellular biology ; Disks Large Homolog 4 Protein ; Fundamental and applied biological sciences. Psychology ; Hippocampus - cytology ; Humanities and Social Sciences ; Humans ; Intracellular Signaling Peptides and Proteins ; Kv1.4 Potassium Channel ; letter ; Membrane Proteins ; Molecular and cellular biology ; Molecular Sequence Data ; multidisciplinary ; Nerve Tissue Proteins - metabolism ; Neurology ; Neurons - metabolism ; Potassium Channels - metabolism ; Potassium Channels, Voltage-Gated ; Proteins ; Rats ; Receptors, N-Methyl-D-Aspartate - genetics ; Receptors, N-Methyl-D-Aspartate - metabolism ; Recombinant Fusion Proteins - metabolism ; Science ; Science (multidisciplinary) ; Space life sciences</subject><ispartof>Nature (London), 1997-01, Vol.385 (6615), p.439-442</ispartof><rights>Springer Nature Limited 1997</rights><rights>1997 INIST-CNRS</rights><rights>Copyright Macmillan Journals Ltd. Jan 30, 1997</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c454t-9ec83f200e2daf8197c3920d5b8a1bf29b18ac2a751436cf9591ff20ab9f70d33</citedby><cites>FETCH-LOGICAL-c454t-9ec83f200e2daf8197c3920d5b8a1bf29b18ac2a751436cf9591ff20ab9f70d33</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,780,784,2727,27924,27925</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=2554617$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/9009191$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Wyszynski, Michael</creatorcontrib><creatorcontrib>Lin, Jerry</creatorcontrib><creatorcontrib>Rao, Anuradha</creatorcontrib><creatorcontrib>Nigh, Elizabeth</creatorcontrib><creatorcontrib>Beggs, Alan H</creatorcontrib><creatorcontrib>Craig, Ann Marie</creatorcontrib><creatorcontrib>Sheng, Morgan</creatorcontrib><title>Competitive binding of α-actinin and calmodulin to the NMDA receptor</title><title>Nature (London)</title><addtitle>Nature</addtitle><addtitle>Nature</addtitle><description>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
1
and dependent on the integrity of actin
2
, suggesting a functionally important interaction between NMDA receptors and the postsynaptic cytoskeleton. α-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. α-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-α-actinin binding is directly antagonized by Ca
2+
/calmodulin. Thus α-actinin may play a role in both the localization of NMDA receptors and their modulation by Ca
2+
.</description><subject>Actins - metabolism</subject><subject>Amino Acid Sequence</subject><subject>Aminoacid receptors (glycine, glutamate, gaba)</subject><subject>Animals</subject><subject>Binding Sites</subject><subject>Binding, Competitive</subject><subject>Biological and medical sciences</subject><subject>Brain</subject><subject>Brain - metabolism</subject><subject>Calmodulin - metabolism</subject><subject>Cell receptors</subject><subject>Cell structures and functions</subject><subject>Cells, Cultured</subject><subject>Cellular biology</subject><subject>Disks Large Homolog 4 Protein</subject><subject>Fundamental and applied biological sciences. 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Academic</collection><jtitle>Nature (London)</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Wyszynski, Michael</au><au>Lin, Jerry</au><au>Rao, Anuradha</au><au>Nigh, Elizabeth</au><au>Beggs, Alan H</au><au>Craig, Ann Marie</au><au>Sheng, Morgan</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Competitive binding of α-actinin and calmodulin to the NMDA receptor</atitle><jtitle>Nature (London)</jtitle><stitle>Nature</stitle><addtitle>Nature</addtitle><date>1997-01-30</date><risdate>1997</risdate><volume>385</volume><issue>6615</issue><spage>439</spage><epage>442</epage><pages>439-442</pages><issn>0028-0836</issn><eissn>1476-4687</eissn><coden>NATUAS</coden><abstract>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
1
and dependent on the integrity of actin
2
, suggesting a functionally important interaction between NMDA receptors and the postsynaptic cytoskeleton. α-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. α-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-α-actinin binding is directly antagonized by Ca
2+
/calmodulin. Thus α-actinin may play a role in both the localization of NMDA receptors and their modulation by Ca
2+
.</abstract><cop>London</cop><pub>Nature Publishing Group UK</pub><pmid>9009191</pmid><doi>10.1038/385439a0</doi><tpages>4</tpages></addata></record> |
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| identifier | ISSN: 0028-0836 |
| ispartof | Nature (London), 1997-01, Vol.385 (6615), p.439-442 |
| issn | 0028-0836 1476-4687 |
| language | eng |
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| source | MEDLINE; Nature; Alma/SFX Local Collection |
| subjects | Actins - metabolism Amino Acid Sequence Aminoacid receptors (glycine, glutamate, gaba) Animals Binding Sites Binding, Competitive Biological and medical sciences Brain Brain - metabolism Calmodulin - metabolism Cell receptors Cell structures and functions Cells, Cultured Cellular biology Disks Large Homolog 4 Protein Fundamental and applied biological sciences. Psychology Hippocampus - cytology Humanities and Social Sciences Humans Intracellular Signaling Peptides and Proteins Kv1.4 Potassium Channel letter Membrane Proteins Molecular and cellular biology Molecular Sequence Data multidisciplinary Nerve Tissue Proteins - metabolism Neurology Neurons - metabolism Potassium Channels - metabolism Potassium Channels, Voltage-Gated Proteins Rats Receptors, N-Methyl-D-Aspartate - genetics Receptors, N-Methyl-D-Aspartate - metabolism Recombinant Fusion Proteins - metabolism Science Science (multidisciplinary) Space life sciences |
| title | Competitive binding of α-actinin and calmodulin to the NMDA receptor |
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