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Research article summary (published 7 Apr 2002):
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NMDA receptor function is regulated by the inhibitory scaffolding protein, RACK1.

Full Abstract

Phosphorylation regulates the function of ligand-gated ion channels such as the N-methyl d-aspartate (NMDA) receptor. Here we report a mechanism for modulation of the phosphorylation state and function of the NMDA receptor via an inhibitory scaffolding protein, RACK1. We found that RACK1 binds both the NR2B subunit of the NMDA receptor and the nonreceptor protein tyrosine kinase, Fyn. RACK1 inhibits Fyn phosphorylation of NR2B and decreases NMDA receptor-mediated currents in CA1 hippocampal slices. Peptides that disrupt the interactions between RACK1, NR2B, and Fyn induce phosphorylation and potentiate NMDA receptor-mediated currents. Therefore, RACK1 is a regulator of NMDA receptor function and may play a role in synaptic plasticity, addiction, learning, and memory.

 

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Author information

Author/s: Yaka, Rami (R); Thornton, Claire (C); Vagts, Alicia J (AJ); Phamluong, Khanhky (K); Bonci, Antonello (A); Ron, Dorit (D);

Affiliation: Ernest Gallo Clinic and Research Center, University of California, San Francisco, CA 94110-3518, USA.

Journal and publication information

Publication Type: Journal Article; Research Support, Non-U.S. Gov't

Journal: Proceedings of the National Academy of Sciences of the United States of America (Proc Natl Acad Sci U S A), published in United States. (Language: eng)

Reference: 2002-Apr; vol 99 (issue 8) : pp 5710-5

Dates: Created 2002/04/17; Completed 2002/06/14; Revised 2006/11/15;

PMID: 11943848, status: MEDLINE (last retrieval date: 11/6/2008)

Sourced from the National Library of Medicine. Abstract text and other information may be subject to copyright.

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MeSH headings (categories)

This article was linked to the MESH Headings shown below.

Associated Chemicals: DNA, Complementary (0) ; GNB2L1 protein, human (0) ; Neoplasm Proteins (0) ; Peptides (0) ; Proto-Oncogene Proteins (0) ; Receptors, Cell Surface (0) ; Receptors, N-Methyl-D-Aspartate (0) ; Recombinant Proteins (0) ; FYN protein, human (EC 2.7.1.112) ; Fyn protein, rat (EC 2.7.1.112) ; Proto-Oncogene Proteins c-fyn (EC 2.7.1.112) ; GTP-Binding Proteins (EC 3.6.1.-)

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