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Titolo:
A use-dependent tyrosine dephosphorylation of NMDA receptors is independent of ion flux
Autore:
Vissel, B; Krupp, JJ; Heinemann, SE; Westbrook, GL;
Indirizzi:
Oregon Hlth Sci Univ, Vollum Inst, Portland, OR 97201 USA Oregon Hlth Sci Univ Portland OR USA 97201 m Inst, Portland, OR 97201 USA Salk Inst Biol Studies, La Jolla, CA 92037 USA Salk Inst Biol Studies La Jolla CA USA 92037 dies, La Jolla, CA 92037 USA
Titolo Testata:
NATURE NEUROSCIENCE
fascicolo: 6, volume: 4, anno: 2001,
pagine: 587 - 596
SICI:
1097-6256(200106)4:6<587:AUTDON>2.0.ZU;2-8
Fonte:
ISI
Lingua:
ENG
Soggetto:
LONG-TERM POTENTIATION; AMPA RECEPTOR; POSTSYNAPTIC DENSITY; SYNAPTIC TRANSMISSION; HIPPOCAMPAL-NEURONS; CHANNEL ACTIVITY; NR1 SUBUNIT; SH2 DOMAINS; PROTEIN; KINASE;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
50
Recensione:
Indirizzi per estratti:
Indirizzo: Krupp, JJ Karolinska Inst, NOVUM, AstraZeneca R&D Sodertalje, Halsovagen 7, S-14157 Huddinge, Sweden Karolinska Inst Halsovagen 7 Huddinge Sweden S-14157 ge, Sweden
Citazione:
B. Vissel et al., "A use-dependent tyrosine dephosphorylation of NMDA receptors is independent of ion flux", NAT NEUROSC, 4(6), 2001, pp. 587-596

Abstract

Tyrosine phosphorylation can upregulate NMDA receptor activity during pathological and physiological alterations of synaptic strength. Here we describe downregulation of recombinant NR1/2A receptors by tyrosine dephosphorylation that requires agonist binding, but is independent of ion flux. The tyrosine residues involved in this new form of NMDA receptor modulation likelyform a 'ring' adjacent to the last transmembrane domain. The downregulation was due to a reduction in the number of functional channels, and was blocked by co-expressing a dominant-negative mu2-subunit of the clathrin-adaptor protein AP-2. Our results provide a mechanism by which synaptic NMDA receptors can be modulated in a use-dependent manner even when the postsynapticmembrane is not sufficiently depolarized to relieve channel block by magnesium ions.

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Documento generato il 26/01/20 alle ore 16:01:34