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Article

PSD-95 promotes Fyn-mediated tyrosine phosphorylation of the N-methyl-D-aspartate receptor subunit NR2A.

Proceedings of the National Academy of Sciences of the United States of America - 19 Jan 1999

Tezuka T, Umemori H, Akiyama T, Nakanishi S, Yamamoto T

Abstract excerpt

Fyn, a member of the Src-family protein-tyrosine kinase (PTK), is implicated in learning and memory that involves N-methyl-D-aspartate (NMDA) receptor function. In this study, we examined how Fyn participates in synaptic plasticity by analyzing the physical and functional interaction between Fyn and NMDA receptors. Results showed that tyrosine phosphorylation of NR2A, one of the NMDA receptor subunits, was...

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Identifiers

PMID: 9892651
DOI: 10.1073/pnas.96.2.435
PMCID: PMC15154

Genes

PSD

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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PSD-95 promotes Fyn-mediated tyrosine phosphorylation of the N-methyl-D-aspartate receptor subunit NR2A.PMID 9892651Read ↗

Characterization of Fyn-mediated tyrosine phosphorylation sites on GluR epsilon 2 (NR2B) subunit of the N-methyl-D-aspartate receptor.Semantic proximity Read ↗

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In vivo composition of NMDA receptor signaling complexes differs between membrane subdomains and is modulated by PSD-95 and PSD-93.Semantic proximity Read ↗

NR2B tyrosine phosphorylation modulates fear learning as well as amygdaloid synaptic plasticity.Semantic proximity Read ↗

The NMDA receptor is coupled to the ERK pathway by a direct interaction between NR2B and RasGRF1.Semantic proximity Read ↗

Blocking Src-PSD-95 interaction rescues glutamatergic signaling dysregulation in schizophreniaSemantic proximity Read ↗

Postsynaptic density 95 (PSD-95) serine 561 phosphorylation regulates a conformational switch and bidirectional dendritic spine structural plasticity.Semantic proximity Read ↗

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