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Titolo:
G protein coupled receptor dimerization: implications in modulating receptor function
Autore:
Gomes, I; Jordan, BA; Gupta, A; Rios, C; Trapaidze, N; Devi, LA;
Indirizzi:
NYU, Sch Med, Dept Pharmacol, New York, NY 10016 USA NYU New York NY USA 10016 Sch Med, Dept Pharmacol, New York, NY 10016 USA
Titolo Testata:
JOURNAL OF MOLECULAR MEDICINE-JMM
fascicolo: 5-6, volume: 79, anno: 2001,
pagine: 226 - 242
SICI:
0946-2716(200106)79:5-6<226:GPCRDI>2.0.ZU;2-1
Fonte:
ISI
Lingua:
ENG
Soggetto:
ANGIOTENSIN-II RECEPTORS; DOPAMINE D2 RECEPTOR; TERMINAL EXTRACELLULAR DOMAIN; BETA-ADRENERGIC RECEPTORS; TACHYKININ NK-1 RECEPTOR; DELTA-OPIOID RECEPTOR; TARGET SIZE ANALYSIS; BINDING-SITES; RADIATION INACTIVATION; BETA(2)-ADRENERGIC RECEPTOR;
Keywords:
opioids; oligomerization; desensitization; signal transduction; downregulation;
Tipo documento:
Review
Natura:
Periodico
Settore Disciplinare:
Clinical Medicine
Life Sciences
Citazioni:
120
Recensione:
Indirizzi per estratti:
Indirizzo: Devi, LA NYU, Sch Med, Dept Pharmacol, 550 1st Ave, New York, NY 10016 USANYU 550 1st Ave New York NY USA 10016 Ave, New York, NY 10016 USA
Citazione:
I. Gomes et al., "G protein coupled receptor dimerization: implications in modulating receptor function", J MOL MED-J, 79(5-6), 2001, pp. 226-242

Abstract

Protein-protein interactions are involved in the regulation of a large number of biological processes. It is well established that a variety of cell surface receptors interact with each other to form dimers, and that this isessential for their activation. Although the existence of G protein coupled receptor dimers was predicted from early pharmacological and biochemical analysis, solid evidence supporting dimerization has come within the past few years following the cloning of G protein coupled receptor cDNAs. Using differential epitope tagging and selective immunoisolation of receptor complexes, dimerization of a number of G protein coupled receptors including members of the rhodopsin, secretin, and metabotropic glutamate receptor families have been reported. More recently fluorescence or bioluminescence resonance energy transfer techniques have been used to examine dimerization of these receptors in live cells. These studies have found that whereas in some cases there is an agonist induced increase in the level of dimers, in others I there is a decrease or no change in dimer levels. Several recent studies have also reported the ability of related members of G protein coupled receptors to heterodimerize. These heterodimers exhibit distinct physical andfunctional properties. Examination of possible sites of interactions between receptors has implicated a role for extracellular, transmembrane and/or C-terminal region in dimerization. The functional consequences of dimerization, explored mainly using mutant receptors, have demonstrated a role in modulating agonist affinity, efficacy, and/or trafficking properties. Thus dimerization appears to be a universal phenomenon that provides an additionalmechanism for modulation of receptor function as well as cross-talk between G protein coupled receptors.

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Documento generato il 23/10/20 alle ore 14:20:54