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Titolo:
A POINT MUTATION IN THE GLUTAMATE BINDING-SITE BLOCKS DESENSITIZATIONOF AMPA RECEPTORS
Autore:
STERNBACH Y; RUSSO S; NEUMAN M; ROSENMUND C;
Indirizzi:
MAX PLANCK INST BIOPHYS CHEM,WORKGRP CELLULAR NEUROBIOL,FASSBERG D-37070 GOTTINGEN GERMANY MAX PLANCK INST BIOPHYS CHEM,WORKGRP CELLULAR NEUROBIOL D-37070 GOTTINGEN GERMANY HEBREW UNIV JERUSALEM,HADASSAH SCH DENT MED,DEPT ANAT & CELL BIOL IL-91120 JERUSALEM ISRAEL MAX PLANCK INST BIOPHYS CHEM,DEPT MEMBRANE BIOPHYS D-37070 GOTTINGEN GERMANY
Titolo Testata:
Neuron (Cambridge, Mass.)
fascicolo: 4, volume: 21, anno: 1998,
pagine: 907 - 918
SICI:
0896-6273(1998)21:4<907:APMITG>2.0.ZU;2-E
Fonte:
ISI
Lingua:
ENG
Soggetto:
CENTRAL NERVOUS-SYSTEM; NEURONAL NICOTINIC RECEPTOR; AMINO-ACID RECEPTORS; METHYL-D-ASPARTATE; SYNAPTIC TRANSMISSION; KAINATE RECEPTORS; HIPPOCAMPAL-NEURONS; CHANNEL DOMAIN; CYCLOTHIAZIDE; ACTIVATION;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Citazioni:
53
Recensione:
Indirizzi per estratti:
Citazione:
Y. Sternbach et al., "A POINT MUTATION IN THE GLUTAMATE BINDING-SITE BLOCKS DESENSITIZATIONOF AMPA RECEPTORS", Neuron (Cambridge, Mass.), 21(4), 1998, pp. 907-918

Abstract

Desensitization of ha-amino-3-hydroxy-5-methyl-4-isoxazole-propionate(AMPA) receptors is thought to shape the synaptic response and act asa neuroprotective mechanism at central synapses, but the molecular mechanism underlying desensitization is poorly understood. We found thatreplacing the glutamate binding domain S1 of GluR3 (an AMPA receptor)with S1 of GluR6 (a kainate receptor) resulted in a fully active but completely nondesensitizing receptor. Smaller substitutions within S1 identified, besides two additional modulatory regions, a single exchange, L507Y, as is required and sufficient for the block, of desensitization. This phenotype was specific for AMPA receptors and required an aromatic residue at this position. L507 lies between two residues (T504and R509) that form part of the glutamate binding site. The physical proximity of these residues, which are involved in binding and gating,suggests they may form part of the link between these two events.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 09/08/20 alle ore 23:15:06