Competitive binding of α-actinin and calmodulin to the NMDA receptor

Michael Wyszynski, Jerry Lin, Anuradha Rao, Elizabeth Nigh, Alan H. Beggs, Ann Marie Craig and Morgan Sheng
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Michael Wyszynski: Massachusetts General Hospital and Harvard Medical School
Jerry Lin: Massachusetts General Hospital and Harvard Medical School
Anuradha Rao: Massachusetts General Hospital and Harvard Medical School
Elizabeth Nigh: Massachusetts General Hospital and Harvard Medical School
Alan H. Beggs: Massachusetts General Hospital and Harvard Medical School
Ann Marie Craig: Massachusetts General Hospital and Harvard Medical School
Morgan Sheng: Massachusetts General Hospital and Harvard Medical School

Nature, 1997, vol. 385, issue 6615, 439-442

Abstract: 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 mechanosensitive1 and dependent on the integrity of actin2, 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 Ca2+/calmodulin. Thus α-actinin may play a role in both the localization of NMDA receptors and their modulation by Ca2+.

Date: 1997
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DOI: 10.1038/385439a0

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