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Cited by 596Neuroscience and Neuropharmacology ResearchGenetics and Neurodevelopmental DisordersReceptor Mechanisms and Signaling

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

Wyszynski, Michael, Lin, Jerry, Rao, Anuradha, Nigh, Elizabeth, Beggs, Alan H., Craig, Ann Marie, Sheng, Morgan·1997·Nature
DOI 10.1038/385439a0
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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 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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Crossref · 10.1038/385439a0

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1 of 1 references verified0 citation errors · 0 not checkable

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  • F-actin is highly concentrated in dendritic spines, appearing as intense punctae along dendrites.

    “Staining of cultured neurons with rhodamine-phalloidin suggests that F-actin is highly concentrated in spines, appearing as intense punctae along the dendrites (Kaech et al., 1997;Wyszynski et al., 1997).”

    From Regulation of F-Actin Stability in Dendritic Spines by Glutamate Receptors and Calcineurin (1998) · cites this paper as Wyszynski et al., 1997

  • NMDA receptors are linked to the actin cytoskeleton via the actin-binding protein α-actinin.

    “Recent findings indicate that NMDA receptors are linked to the actin cytoskeleton via the actin-binding protein ␣-actinin (Wyszynski et al., 1997).”

    From Regulation of F-Actin Stability in Dendritic Spines by Glutamate Receptors and Calcineurin (1998) · cites this paper as Wyszynski et al., 1997

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Authors
Wyszynski, M., Lin, J., Rao, A., Nigh, E., Beggs, A. H., Craig, A. M., & Sheng, M.
Affiliations
Howard Hughes Medical Institute (US)
ORCID
Venue
Nature
Publisher
Springer Science and Business Media LLC
Published
1997-01
Volume
385
Issue
6615
Pages
439-442
ISSN
  • 0028-0836 (ISSN-L)
  • 1476-4687
DOI
10.1038/385439a0
OpenAlex
W1972884505
Cited by
596
References
1
Citations by year
2026: 4 · 2025: 3 · 2024: 4 · 2023: 4 · 2022: 5 · 2021: 6 · 2020: 10 · 2019: 8 · 2018: 10 · 2017: 5 · 2016: 11 · 2015: 12 · 2014: 19 · 2013: 15 · 2012: 20
FWCI
23.76
Type
journal article
Language
en
Open access
closed
Licence
www.springer.com/tdm (tdm)
Locations
  • Nature (publishedVersion)
  • PubMed (publishedVersion)
  • RePEc: Research Papers in Economics (submittedVersion)
Topics
  • Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Neuroscience and Neuropharmacology Research
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Genetics › Genetics and Neurodevelopmental Disorders
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Receptor Mechanisms and Signaling
Keywords
NMDA receptor, ACTN2, calmodulin, PSD-95, postsynaptic density, dendritic spines, receptor immobilization, NR1 subunit, NR2B subunit, calcium signaling, receptor clustering, actin-binding proteins
MeSH terms
Disks Large Homolog 4 Protein, Actins, Amino Acid Sequence, Animals, Binding Sites, Binding, Competitive, Brain, Calmodulin, Cells, Cultured, Hippocampus, Humans, Membrane Proteins, Molecular Sequence Data, Nerve Tissue Proteins, Neurons, Recombinant Fusion Proteins, Potassium Channels, Receptors, N-Methyl-D-Aspartate, Potassium Channels, Voltage-Gated, Intracellular Signaling Peptides and Proteins, Rats, Kv1.4 Potassium Channel

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