RT Journal Article
SR Electronic
T1 Control of assembly and function of glutamate receptors by the amino-terminal domain
JF Molecular Pharmacology
JO Mol Pharmacol
FD American Society for Pharmacology and Experimental Therapeutics
SP mol.110.067157
DO 10.1124/mol.110.067157
A1 Kasper B Hansen
A1 Hiro Furukawa
A1 Stephen F. Traynelis
YR 2010
UL http://molpharm.aspetjournals.org/content/early/2010/07/21/mol.110.067157.abstract
AB The extracellular amino-terminal domains of the ionotropic glutamate receptor subunits form a semi-autonomous 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.