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Article

Stabilization of Ca2+-permeable AMPA receptors at perisynaptic sites by GluR1-S845 phosphorylation.

Proceedings of the National Academy of Sciences of the United States of America - 24 Nov 2009

He Kaiwen, Song Lihua, Cummings Laurel W, Goldman Jonathan, Huganir Richard L, Lee Hey-Kyoung

Abstract excerpt

AMPA receptor (AMPAR) channel properties and function are regulated by its subunit composition and phosphorylation. Certain types of neural activity can recruit Ca(2+)-permeable (CP) AMPARs, such as GluR1 homomers, to synapses likely via lateral diffusion from extrasynaptic sites. Here we show that GluR1-S845 phosphorylation can alter the subunit composition of perisynaptic AMPARs by providing stability to GluR1...

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Identifiers

PMID: 19892736
DOI: 10.1073/pnas.0910338106
PMCID: PMC2785287

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 6 Sept 2026. Manifest publication-graph-cohort-2026-09-06.1.

Source receipt: pubmed, retrieved 6 Sept 2026.

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