Research article summary (published 30 Mar 1996):

Interaction between the C terminus of NMDA receptor subunits and multiple members of the PSD-95 family of membrane-associated guanylate kinases.

Full Abstract

Selective concentration and anchoring of ionotropic receptors at the synapse is essential for neuronal signaling. Little is known about the molecules that mediate receptor clustering in the CNS. With use of the yeast two-hybrid system to screen a rat brain cDNA library and by in vitro binding assays, we have identified an interaction between NMDA receptor subunits 2A and 2B (NR2A and NR2B) and three distinct members of the PSD-95/SAP90 family of membrane-associated putative guanylate kinases. The interaction is mediated by binding of the C terminus of the NMDA receptor subunits to the first two PDZ (also known as GLGF or DHR) domains of PSD-95/SAP90, an abundant synaptic protein associated with the membrane cytoskeleton. PSD-95 is also known to bind and cluster Shaker-type voltage-gated K+ channels. Similarities between the C-termini of NR2 subunits and K+ channels suggest a common C-terminal binding motif for PDZ domains. These data suggest that PDZ domains can function as modules for protein-protein interactions. Members of the PSD-95 family might serve to anchor NMDA receptors to the submembrane cytoskeleton and aid in the assembly of signal transduction complexes at postsynaptic sites.

Author information

Author/s: Niethammer, M (M); Kim, E (E); Sheng, M (M);

Affiliation: Department of Neurobiology, Harvard Medical School, Boston, Massachusetts 02114, USA.

Journal and publication information

Publication Type: Journal Article

Journal: The Journal of neuroscience : the official journal of the Society for Neuroscience (J Neurosci), published in UNITED STATES. (Language: eng)

Reference: 1996-Apr; vol 16 (issue 7) : pp 2157-63

Dates: Created 1996/05/09; Completed 1996/05/09; Revised 2005/11/17;

PMID: 8601796, status: MEDLINE (last retrieval date: 2/18/2009, IMS Date: )

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.

Animals Brain Chemistry Cell Membrane - enzymology DNA, Complementary - physiology Gene Library Guanylate Kinase Intracellular Signaling Peptides and Proteins Membrane Proteins Molecular Sequence Data

Nerve Tissue Proteins - metabolism Nucleoside-Phosphate Kinase - metabolism Potassium Channels - metabolism; ultrastructure Protein Binding - physiology Rats Receptors, N-Methyl-D-Aspartate - metabolism; ultrastructure Sequence Homology, Amino Acid Synapses - metabolism; ultrastructure Yeasts - enzymology; ultrastructure

Associated Chemicals: DNA, Complementary (0) ; Dlgh4 protein, rat (0) ; Intracellular Signaling Peptides and Proteins (0) ; Membrane Proteins (0) ; Nerve Tissue Proteins (0) ; Potassium Channels (0) ; Receptors, N-Methyl-D-Aspartate (0) ; postsynaptic density proteins (0) ; Nucleoside-Phosphate Kinase (EC 2.7.4.4) ; Guanylate Kinase (EC 2.7.4.8)

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