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Titolo:
DIFFERENTIAL ROLE OF THE CARBOXYL-TERMINAL TYROSINE IN DOWN-REGULATION AND SEQUESTRATION OF THE M2 MUSCARINIC ACETYLCHOLINE-RECEPTOR
Autore:
GOLDMAN PS; NATHANSON NM;
Indirizzi:
UNIV WASHINGTON,DEPT PHARMACOL,SJ 30 SEATTLE WA 98195 UNIV WASHINGTON,DEPT PHARMACOL SEATTLE WA 98195
Titolo Testata:
The Journal of biological chemistry
fascicolo: 22, volume: 269, anno: 1994,
pagine: 15640 - 15645
SICI:
0021-9258(1994)269:22<15640:DROTCT>2.0.ZU;2-G
Fonte:
ISI
Lingua:
ENG
Soggetto:
BETA-ADRENERGIC-RECEPTOR; DENSITY-LIPOPROTEIN RECEPTOR; NEURO-BLASTOMA CELLS; CULTURED HEART-CELLS; CHOLINERGIC RECEPTORS; CYTOPLASMIC DOMAIN; BINDING PROTEIN; INTERNALIZATION; ENDOCYTOSIS; AGONIST;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Citazioni:
42
Recensione:
Indirizzi per estratti:
Citazione:
P.S. Goldman e N.M. Nathanson, "DIFFERENTIAL ROLE OF THE CARBOXYL-TERMINAL TYROSINE IN DOWN-REGULATION AND SEQUESTRATION OF THE M2 MUSCARINIC ACETYLCHOLINE-RECEPTOR", The Journal of biological chemistry, 269(22), 1994, pp. 15640-15645

Abstract

Muscarinic acetylcholine receptor (mAChR) number can be altered in response to sustained agonist exposure. Short term agonist exposure (seconds to minutes) causes a rapid removal of mAChR from the cell surface(sequestration) while agonist exposure for longer periods of time (hours) causes a decrease in total receptor number (down-regulation). Tyrosine residues located in the cytoplasmic tails of a number of membrane receptors have been demonstrated to be important in the regulation by either sequestration, as is the case with the mannose 6-phosphate receptor and other receptors endocytosed via clathrin coated vesicles, or down-regulation, as is the case with the beta(2)-adrenergic receptor. Mutation of the lone cytoplasmic tail tyrosine residue (Tyr-459) of the mammalian m2 mAChR to Phe, Trp, or Ala did not affect agonist-induced sequestration, although it significantly attenuated agonist-induced down-regulation. Conversion of m2 Tyr-459 to lie did not affect the rate or extent of agonist-induced sequestration or down-regulation, but the sensitivity of this mutant receptor to agonist-induced down-regulation was slightly decreased. Agonist and antagonist binding as well as functional coupling to the inhibition of cAMP accumulation was unaffected by any of the mutations to Tyr-459. These results are the firstto identify a site in a mAChR involved in the down-regulation of receptor in response to agonist.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 27/11/20 alle ore 07:29:01