|
|
| Research article summary (published 7 Apr 2002): |
|
Free Full Text! See links below |
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.
Learn Faster Today Improve your study skills
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.
External Links for this article (including full text providers, if available):
Click Electronic Full-text Provider Links to see options for finding the electronic full text links to this article. Note there may be a subscription or fee required for access to the full text. See our FAQ for information on finding FREE full text articles.
This article may also be located in paper journal collections available in many libraries. Use the Journal and Publication Information above to find the full article.
MeSH headings (categories)
This article was linked to the MESH Headings shown below.
|
|
Related articles
This article has not been indexed for related articles as yet, however you can still use the live related article search links below.
See a large map of 100+ related articles.