Glutamate receptor subunit 2 serine 880 phosphorylation modulates synaptic transmission and mediates plasticity in CA1 pyramidal cells

Seidenman, K. J., Steinberg, J. P., Huganir, R., Malinow, R. (October 2003) Glutamate receptor subunit 2 serine 880 phosphorylation modulates synaptic transmission and mediates plasticity in CA1 pyramidal cells. Journal of Neuroscience, 23 (27). pp. 9220-9228. ISSN 0270-6474

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URL: http://www.ncbi.nlm.nih.gov/pubmed/14534256

Abstract

The cytoplasmic C termini of AMPA receptor subunits contain PDZ ( postsynaptic density 95/Discs large/zona occludens 1) ligand domains that can control their synaptic trafficking during plasticity. The glutamate receptor subunit 2 (GluR2) PDZ ligand domain can be phosphorylated at serine 880 (S880), and this disrupts interactions with GRIP/ABP (glutamate receptor-interacting protein/AMPA binding protein) but not with PICK1 (PKC-interacting protein 1). Here, the impact of GluR2 S880 phosphorylation on synaptic transmission and plasticity was explored by expressing, in hippocampal slice cultures, GluR2 subunits containing point mutations that mimic or prevent phosphorylation at this residue. Our results indicate that mimicking GluR2 S880 phosphorylation excludes these receptors from synapses, depresses transmission, and partially occludes long-term depression (LTD). Conversely, mutations that prevent phosphorylation reduce LTD. Disruption of the interaction between GluR2 and GRIP/ABP by S880 phosphorylation may thus facilitate removal of synaptic AMPA receptors and mediate some forms of activity-dependent synaptic depression.

Item Type:	Paper
Uncontrolled Keywords:	AMPA LTD hippocampus synapse plasticity trafficking PROTEIN-KINASE-C LONG-TERM DEPRESSION DOMAIN-CONTAINING PROTEINS AMPA RECEPTOR BINDING-PROTEIN INTERACTING PROTEIN DIFFERENTIAL PALMITOYLATION HIPPOCAMPAL LTD GLUR2 PICK1
Subjects:	bioinformatics > genomics and proteomics > genetics & nucleic acid processing > protein structure, function, modification > protein types > AMPA receptor bioinformatics > genomics and proteomics > genetics & nucleic acid processing bioinformatics > genomics and proteomics > genetics & nucleic acid processing > protein structure, function, modification bioinformatics > genomics and proteomics > genetics & nucleic acid processing > protein structure, function, modification > protein types > glutamate receptor organs, tissues, organelles, cell types and functions > tissues types and functions > hippocampus organs, tissues, organelles, cell types and functions bioinformatics > genomics and proteomics > genetics & nucleic acid processing > protein structure, function, modification > protein expression > phosphorylation bioinformatics > genomics and proteomics > genetics & nucleic acid processing > protein structure, function, modification > protein expression bioinformatics > genomics and proteomics > genetics & nucleic acid processing > protein structure, function, modification > protein types organs, tissues, organelles, cell types and functions > tissues types and functions
CSHL Authors:	Malinow, Roberto Seidenman, Kenneth
Communities:	CSHL labs > Malinow lab
Depositing User:	Matt Covey
Date:	October 2003
Date Deposited:	02 Apr 2013 14:00
Last Modified:	02 Apr 2013 14:00
Related URLs:	Publisher
URI:	https://repository.cshl.edu/id/eprint/27992

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