Control of assembly and function of glutamate receptors by the amino-terminal domain

Kasper B. Hansen, Hiro Furukawa, Stephen F. Traynelis

Research output: Contribution to journalShort surveypeer-review

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.

Original languageEnglish
Pages (from-to)535-549
Number of pages15
JournalMolecular Pharmacology
Volume78
Issue number4
DOIs
StatePublished - Oct 2010

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