Control of Assembly and Function of Glutamate Receptors by the Amino-Terminal Domain

Hansen, K. B., Furukawa, H., Traynelis, S. F. (2010) Control of Assembly and Function of Glutamate Receptors by the Amino-Terminal Domain. Molecular Pharmacology, 78 (4). pp. 535-549. ISSN 0026-895X

URL: http://www.ncbi.nlm.nih.gov/pubmed/20660085
DOI: 10.1124/mol.110.067157

Abstract

The extracellular amino-terminal domains (ATDs) of the ionotropic glutamate receptor subunits form a semiautonomous component of all glutamate receptors that resides distal to the membrane and controls a surprisingly diverse set of receptor functions. These functions include subunit assembly, receptor trafficking, channel gating, agonist potency, and allosteric modulation. The many divergent features of the different ionotropic glutamate receptor classes and different subunits within a class may stem from differential regulation by the amino-terminal domains. The emerging knowledge of the structure and function of the amino-terminal domains reviewed here may enable targeting of this region for the therapeutic modulation of glutamatergic signaling. Toward this end, NMDA receptor antagonists that interact with the GluN2B ATD show promise in animal models of ischemia, neuropathic pain, and Parkinson's disease.

Item Type: Paper
Uncontrolled Keywords: METHYL-D-ASPARTATE Methyl D-Aspartate RECOMBINANT NMDA RECEPTORS Recombinant NMDA receptors LIGAND-BINDING DOMAIN ligand binding domain MOUSE HIPPOCAMPAL-NEURONS mouse hippocampal neurons CULTURED CORTICAL-NEURONS cultured cortican neurons CONE HORIZONTAL cone horizontal CELLS cells NR2B SUBUNIT subunit ZINC INHIBITION zinc inhibition ENDOPLASMIC-RETICULUM endoplasmic reticulum KAINATE kainate RECEPTORS receptors
Subjects: bioinformatics > genomics and proteomics > small molecules > NMDA receptor
bioinformatics > genomics and proteomics > genetics & nucleic acid processing > protein structure, function, modification > protein types > ionotropic glutamate receptor
bioinformatics > genomics and proteomics > genetics & nucleic acid processing > protein structure, function, modification > protein structure rendering
CSHL Authors:
Communities: CSHL labs > Furukawa lab
Depositing User: Leigh Johnson
Date Deposited: 26 Mar 2012 18:02
Last Modified: 04 Feb 2015 20:49
PMCID: PMC2981397
Related URLs:
URI: http://repository.cshl.edu/id/eprint/25160

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