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Titolo:
Alteration in ion channel function of mouse nicotinic acetylcholine receptor by mutations in the M4 transmembrane domain
Autore:
Tamamizu, S; Lee, YH; Hung, B; McNamee, MG; Lasalde-Dominicci, JA;
Indirizzi:
Univ Puerto Rico, Dept Biol, Rio Piedras, PR 00931 USA Univ Puerto Rico Rio Piedras PR USA 00931 Biol, Rio Piedras, PR 00931 USA Univ Calif Davis, Sect Mol & Cellular Biol, Davis, CA 95616 USA Univ CalifDavis Davis CA USA 95616 & Cellular Biol, Davis, CA 95616 USA
Titolo Testata:
JOURNAL OF MEMBRANE BIOLOGY
fascicolo: 2, volume: 170, anno: 1999,
pagine: 157 - 164
SICI:
0022-2631(19990715)170:2<157:AIICFO>2.0.ZU;2-E
Fonte:
ISI
Lingua:
ENG
Soggetto:
LIPID-PROTEIN INTERFACE; AFFINITY BINDING-SITE; H-3 CHLORPROMAZINE; DELTA-SUBUNIT; NONCOMPETITIVE BLOCKERS; SECONDARY STRUCTURE; GATING KINETICS; ALPHA-SUBUNIT; AMINO-ACIDS; RESIDUES;
Keywords:
Torpedo californica; cassette mutagenesis; single channel electrophysiology; ion channel gating;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
36
Recensione:
Indirizzi per estratti:
Indirizzo: Lasalde-Dominicci, JA Univ Puerto Rico, Dept Biol, POB 23360, Rio Piedras,PR 00931 USA Univ Puerto Rico POB 23360 Rio Piedras PR USA 00931
Citazione:
S. Tamamizu et al., "Alteration in ion channel function of mouse nicotinic acetylcholine receptor by mutations in the M4 transmembrane domain", J MEMBR BIO, 170(2), 1999, pp. 157-164

Abstract

The effect of structural alterations of the M4 transmembrane segment in the Torpedo californica AChR has shown that substitution of specific residuescan be critical to the channel gating (Lasalde et al., 1996). In a previous study we found that phenylalanine and tryptophan substitutions at the alpha C418 residue in the M4 transmembrane segment of the Torpedo californica AChR significantly altered ion channel function (Lee et al., 1994; Ortiz-Miranda et al., 1997). Cassette mutagenesis was used to mutate the Cys residue at the corresponding C418 position in the alpha subunit of mouse AChR. A total of nine mutations on the mouse alpha C418 position were tested, including the alpha C418A, alpha C418V, alpha C418L, alpha C418S, alpha C418M, alpha C418W, alpha C418H, alpha C418E and alpha C418G mutants. All the mutants tested were functional except the alpha C418G which was not expressed onthe surface of the oocyte. The data obtained from macroscopic and single channel currents demonstrate that different types of amino acids can be accommodated at this presumably lipid-exposed position without loss of ion-channel function. As with the Torpedo AChR, the mutation of Cys to Trp dramatically decreased the EC50 for acetylcholine and increased channel open time. The lack of expression of the mouse alpha C418G suggest that there are somedifferences in folding, oligomerization and perhaps transport to the surface membrane for this mutant between the Torpedo and the mammalian AChR.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 23/09/20 alle ore 09:16:55