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Author Notes:

Address correspondence to: Dr. Stephen F. Traynelis, Department of Pharmacology, Emory University School of Medicine, Rollins Research Center, 1510 Clifton Road, Atlanta GA 30322-3090, Tel: (+1) 404 727 0357, Fax: (+1) 404 727 0365, E-mail: strayne@emory.edu

S.F.T. holds an equity position in NeurOp Inc.


Research Funding:

This work was supported by the National Institutes of Health National Institute of Neurological Disorders and Stroke [Grants NS036654, NS065371]; National Institutes of Health National Institute of Mental Health [Grant MH085926-01A1]; the Alzheimer's Association; the Lundbeck Foundation; and the Villum Kann Rasmussen Foundation.

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


Journal Title:

Molecular Pharmacology


Volume 78, Number 4


, Pages 535-549

Type of Work:

Article | Post-print: After Peer Review


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.

Copyright information:

© 2010 The American Society for Pharmacology and Experimental Therapeutics

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