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Titolo:
Interaction between transmembrane domains five and six of the alpha-factorreceptor
Autore:
Dube, P; DeCostanzo, A; Konopka, JB;
Indirizzi:
SUNY Stony Brook, Dept Mol Genet & Microbiol, Stony Brook, NY 11794 USA SUNY Stony Brook Stony Brook NY USA 11794 biol, Stony Brook, NY 11794 USA SUNY Stony Brook, Mol & Cellular Biol Program, Stony Brook, NY 11794 USA SUNY Stony Brook Stony Brook NY USA 11794 gram, Stony Brook, NY 11794 USA
Titolo Testata:
JOURNAL OF BIOLOGICAL CHEMISTRY
fascicolo: 34, volume: 275, anno: 2000,
pagine: 26492 - 26499
SICI:
0021-9258(20000825)275:34<26492:IBTDFA>2.0.ZU;2-1
Fonte:
ISI
Lingua:
ENG
Soggetto:
PROTEIN-COUPLED RECEPTORS; FACTOR PHEROMONE RECEPTOR; DOMINANT-NEGATIVE MUTATIONS; MEMBRANE-SPANNING SEGMENT; DOPAMINE D2 RECEPTOR; BINDING-SITE CREVICE; SACCHAROMYCES-CEREVISIAE; SCANNING MUTAGENESIS; LIGAND SPECIFICITY; PLASMA-MEMBRANE;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
46
Recensione:
Indirizzi per estratti:
Indirizzo: Konopka, JB SUNY Stony Brook, Dept Mol Genet & Microbiol, Stony Brook, NY 11794 USA SUNY Stony Brook Stony Brook NY USA 11794 Brook, NY 11794 USA
Citazione:
P. Dube et al., "Interaction between transmembrane domains five and six of the alpha-factorreceptor", J BIOL CHEM, 275(34), 2000, pp. 26492-26499

Abstract

The a-factor pheromone receptor (STE2) activates a G protein signal pathway that induces conjugation of the yeast Saccharomyces cerevisiae, Previous studies implicated the third intracellular loop of this receptor in G; protein activation. Therefore, the roles of transmembrane domains five and six (TMD5 and -6) that bracket the third intracellular loop were analyzed by scanning mutagenesis in which each residue was substituted with cysteine. Outof 42 mutants examined, four constitutive mutants and two strong loss-of-function mutants were identified, Double mutants combining Cys substitutionsin TMD5 and TMD6 gave a broader range of phenotypes, Interestingly, a V223C mutation in TMD5 caused constitutive activity when combined with the L247C, L248C, or S251C mutations in TMD6, Also, the L226C mutation in TMD5 caused constitutive activity when combined with either the M250C or S251C mutations in TMD6. The residues affected by these mutations are predicted to fall on one side of their respective helices, suggesting that they may interact. In support of this, cysteines substituted at position 223 in TMD5 and position 247 in TMD6 formed a disulfide bond, providing the first direct evidence of an interaction between these transmembrane domains in the ct-factorreceptor. Altogether, these results identify an important region of interaction between conserved hydrophobic regions at the base of TMD5 and TMD6 that is required for the proper regulation of receptor signaling.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 25/01/20 alle ore 03:45:15