Work

Glutamate Receptor Subunit 2 Serine 880 Phosphorylation Modulates Synaptic Transmission and Mediates Plasticity in CA1 Pyramidal Cells

Year: 2003

Type: article

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.

Source: Journal of Neuroscience

DOI: 10.1523/jneurosci.23-27-09220.2003

Authors: Kenneth J. Seidenman, Jordan P. Steinberg, Richard Huganir, Roberto Malinow

Institutions: Howard Hughes Medical Institute, Johns Hopkins University, Cold Spring Harbor Laboratory

Language: English

Topic: Neuroscience and Neuropharmacology Research

Subfield: Cellular and Molecular Neuroscience

Field: Neuroscience

Domain: Life Sciences

Open Access status: bronze

Funder: National Institutes of Health

OpenAlex ID: W1805816820