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Titolo:
Effects of mutation at a conserved N-glycosylation site in the bovine retinal cyclic nucleotide-gated ion channel
Autore:
Rho, SH; Lee, HM; Lee, K; Park, CS;
Indirizzi:
Kwangju Inst Sci & Technol, Dept Life Sci, Kwangju 500712, South Korea Kwangju Inst Sci & Technol Kwangju South Korea 500712 00712, South Korea Ewha Womans Univ, Coll Pharm, Seoul 120750, South Korea Ewha Womans Univ Seoul South Korea 120750 arm, Seoul 120750, South Korea
Titolo Testata:
FEBS LETTERS
fascicolo: 3, volume: 478, anno: 2000,
pagine: 246 - 252
SICI:
0014-5793(20000804)478:3<246:EOMAAC>2.0.ZU;2-H
Fonte:
ISI
Lingua:
ENG
Soggetto:
SHAKER K+ CHANNEL; ELECTROSTATIC INTERACTIONS; FUNCTIONAL EXPRESSION; EPITHELIAL-CELLS; POTASSIUM; SUBUNIT; BINDING; PORE; SENSITIVITY; CONDUCTANCE;
Keywords:
N-glycosylation; cyclic nucleotide-gated ion channel; guanosine 3 ',5 '-cyclic mononucleotide; divalent cation blockade; Xenopus oocyte;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
33
Recensione:
Indirizzi per estratti:
Indirizzo: Park, CS Kwangju Inst Sci & Technol, Dept Life Sci, Kwangju 500712, South Korea Kwangju Inst Sci & Technol Kwangju South Korea 500712 uth Korea
Citazione:
S.H. Rho et al., "Effects of mutation at a conserved N-glycosylation site in the bovine retinal cyclic nucleotide-gated ion channel", FEBS LETTER, 478(3), 2000, pp. 246-252

Abstract

Bovine retinal cyclic nucleotide-gated (CSG) ion channel contains an evolutionary conserved N-glycosylation site in the external loop between the fifth transmembrane segment and the pore-forming region. The effect of tunicamycin treatment and the site-specific mutation suggested that the channel isglycosylated when expressed in Xenopus oocytes, To test the role of glycosylation in this channel, N-glycosylation was abolished by mutation, and thedetailed permeation and the gating characteristics of the mutant channel mere investigated. The charge contribution turned out to be detectable, although the mutation of the N-glycosylation site did not affect expression andfunctionality of the CNG channel in oocytes, (C) 2000 Federation of European Biochemical Societies. Published by Elsevier Science B.V. All rights reserved.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 29/05/20 alle ore 03:58:12