Catalogo Articoli (Spogli Riviste)

OPAC HELP

Titolo:
The Lurcher mutation reveals Ca2+ permeability and PKC modification of theGluR delta channels
Autore:
Ikeno, K; Yamakura, T; Yamazaki, M; Sakimura, K;
Indirizzi:
Niigata Univ, Brain Res Inst, Dept Cellular Neurobiol, Niigata 9518585, Japan Niigata Univ Niigata Japan 9518585 lar Neurobiol, Niigata 9518585, Japan Niigata Univ, Sch Med, Dept Anesthesiol, Niigata 9518510, Japan Niigata Univ Niigata Japan 9518510 t Anesthesiol, Niigata 9518510, Japan
Titolo Testata:
NEUROSCIENCE RESEARCH
fascicolo: 2, volume: 41, anno: 2001,
pagine: 193 - 200
SICI:
0168-0102(200110)41:2<193:TLMRCP>2.0.ZU;2-S
Fonte:
ISI
Lingua:
ENG
Soggetto:
NMDA RECEPTOR-CHANNEL; XENOPUS OOCYTES; PURKINJE-CELLS; CLONED CDNAS; SUBUNIT; PHOSPHORYLATION; EXPRESSION; INTERACTS; MUTANT; DOMAIN;
Keywords:
glutamate receptor delta subunit; Lurcher mutation; Ca2+ permeability; PKC; channel gating;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
32
Recensione:
Indirizzi per estratti:
Indirizzo: Sakimura, K Niigata Univ, Brain Res Inst, Dept Cellular Neurobiol, 1 Asahimachi Dori, Niigata 9518585, Japan Niigata Univ 1 Asahimachi Dori Niigata Japan 9518585 5, Japan
Citazione:
K. Ikeno et al., "The Lurcher mutation reveals Ca2+ permeability and PKC modification of theGluR delta channels", NEUROSCI RE, 41(2), 2001, pp. 193-200

Abstract

The physiological function of the GluR delta subfamily which is one of theglutamate receptor (GluR) channel subunits has not vet been clarified. because no GluR channel activity has been detected in heterologous expression systems. The Lurcher mutation, a point mutation of the GluR delta2 subunit,converts it into a constitutively active and cation-permeating channel. Weintroduced this mutation into GluR delta1 and GluR delta2. AMPA-selective,and NMDA-selective GluR channel subunits. and characterized their channel properties. It was shown that the Lurcher mutation alters the gating properties of AMPA- and NMDA-selective GluR channels. but not their cation permeabilities nor metabolic modulations. These findings support the idea that the Lurcher mutant homomeric GluR delta1 channels are permeable to Ca2+ as dothe mutant GluR delta2 channels, reflecting their original channel properties. We also found that cation permeability of the mutant GluR delta1 channels was decreased by TPA, a protein kinase C activator. It indicates the possibility that phosphorylation by PKC activation may inhibit channel with wild-type GluR delta1 subunit. (C) 2001 Published by Elsevier Science Ireland Ltd.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 29/03/20 alle ore 08:58:56