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Titolo:
Subunit interactions and AMPA receptor desensitization
Autore:
Robert, A; Irizarry, SN; Hughes, TE; Howe, JR;
Indirizzi:
Yale Univ, Sch Med, Dept Pharmacol, New Haven, CT 06520 USA Yale Univ NewHaven CT USA 06520 Dept Pharmacol, New Haven, CT 06520 USA Yale Univ, Sch Med, Dept Ophthalmol, New Haven, CT 06520 USA Yale Univ New Haven CT USA 06520 Dept Ophthalmol, New Haven, CT 06520 USA
Titolo Testata:
JOURNAL OF NEUROSCIENCE
fascicolo: 15, volume: 21, anno: 2001,
pagine: 5574 - 5586
SICI:
0270-6474(20010801)21:15<5574:SIAARD>2.0.ZU;2-B
Fonte:
ISI
Lingua:
ENG
Soggetto:
GLUTAMATE-OPERATED CHANNELS; NUCLEOTIDE-GATED CHANNEL; LIGAND-BINDING CORE; SYNAPTIC TRANSMISSION; KAINATE RECEPTORS; HIPPOCAMPAL-NEURONS; ION CHANNELS; CYCLOTHIAZIDE; ACTIVATION; MODULATION;
Keywords:
glutamate; AMPA receptor; desensitization; subunit interactions; allosteric; kinetics;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
46
Recensione:
Indirizzi per estratti:
Indirizzo: Howe, JR Yale Univ, Sch Med, Dept Pharmacol, 333 Cedar St, New Haven, CT 06520 USA Yale Univ 333 Cedar St New Haven CT USA 06520 Haven, CT 06520 USA
Citazione:
A. Robert et al., "Subunit interactions and AMPA receptor desensitization", J NEUROSC, 21(15), 2001, pp. 5574-5586

Abstract

Most AMPA-type glutamate receptors (GluRs) exhibit rapid and virtually complete desensitization when activated by glutamate, and at some central synapses it is largely desensitization that determines the decay of EPSCs. However, the mechanisms underlying the conformation change that results in desensitization are not fully understood. AMPA receptor subunits that contain asingle amino acid substitution have been shown to form homomeric channels that show markedly reduced desensitization. We show here that the coexpression of wild-type GluR1 with one such mutant, GluR1( L497Y), results in heteromeric channels that show desensitization behavior that is intermediate between wild-type and mutant homomers. The relative amplitudes of the multiple exponential components present in the decay of glutamate-evoked currents depended on the relative abundance of wild-type and mutant subunits and were described by the combinatorial distribution of the two types of subunits into tetrameric, but not pentameric, assemblies. Our results are consistentwith recent structural data suggesting that AMPA receptors are tetrameric assemblies composed of two dimers.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 06/04/20 alle ore 08:41:21