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Titolo:
Differential affinities of visual arrestin, beta arrestin1, and beta arrestin2 for G protein-coupled receptors delineate two major classes of receptors
Autore:
Oakley, RH; Laporte, SK; Holt, JA; Caron, MG; Barak, LS;
Indirizzi:
Duke Univ, Med Ctr, Dept Cell Biol, Howard Hughes Med Inst Labs, Durham, NC 27710 USA Duke Univ Durham NC USA 27710 Hughes Med Inst Labs, Durham, NC 27710 USA Duke Univ, Med Ctr, Dept Med, Howard Hughes Med Inst Labs, Durham, NC 27710 USA Duke Univ Durham NC USA 27710 Hughes Med Inst Labs, Durham, NC 27710 USA
Titolo Testata:
JOURNAL OF BIOLOGICAL CHEMISTRY
fascicolo: 22, volume: 275, anno: 2000,
pagine: 17201 - 17210
SICI:
0021-9258(20000602)275:22<17201:DAOVAB>2.0.ZU;2-C
Fonte:
ISI
Lingua:
ENG
Soggetto:
BETA-ADRENERGIC-RECEPTOR; CLATHRIN-MEDIATED ENDOCYTOSIS; PROSTAGLANDIN E-2 RECEPTORS; BETA(2)-ADRENERGIC RECEPTOR; WILD-TYPE; RHODOPSIN; KINASE; BINDING; DESENSITIZATION; RESENSITIZATION;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
43
Recensione:
Indirizzi per estratti:
Indirizzo: Caron, MG Duke Univ, Med Ctr, Howard Hughes Med Inst, Box 3287, Durham, NC27710 USA Duke Univ Box 3287 Durham NC USA 27710 287, Durham, NC 27710 USA
Citazione:
R.H. Oakley et al., "Differential affinities of visual arrestin, beta arrestin1, and beta arrestin2 for G protein-coupled receptors delineate two major classes of receptors", J BIOL CHEM, 275(22), 2000, pp. 17201-17210

Abstract

Visual arrestin, beta arrestin1, and beta arrestin2 comprise a family of intracellular proteins that desensitize G protein-coupled receptors (GPCRs),In addition, beta arrestin1 and beta arrestin2 target desensitized receptors to clathrin-coated pits for endocytosis. Whether arrestins differ in their ability to interact with GPCRs in cells is not known, In this study, we visualize the interaction of arrestin family members with GPCRs in real time and in live cells using green fluorescent protein-tagged arrestins, In the absence of agonist, visual arrestin and beta arrestin1 were found in boththe cytoplasm and nucleus of HEK-293 cells, whereas beta arrestin2 was found only in the cytoplasm. Analysis of agonist-mediated arrestin translocation to multiple GPCRs identified two major classes of receptors, Class A receptors (beta 2 adrenergic receptor, mu opioid receptor, endothelin type A receptor, dopamine D1A receptor, and alb adrenergic receptor) bound beta arrestin2 with higher affinity than beta arrestin1 and did not interact with visual arrestin, In contrast, class B receptors (angiotensin II type 1A receptor, neurotensin receptor 1, vasopressin V2 receptor, thyrotropin-releasing hormone receptor, and substance P receptor) bound both beta arrestin isoforms with similar high affinities and also interacted with visual arrestin. Switching the carboxyl-terminal tails of class A and class B receptors completely reversed the affinity of each receptor for the visual and non-visual arrestins, In addition, exchanging the beta arrestin1 and beta arrestin2 carboxyl termini reversed their extent of binding to class A receptors as well as their subcellular distribution. These results reveal for the first time marked differences in the ability of arrestin family members to bind GPCRs at the plasma membrane, Moreover, they show that visual arrestin can interact in cells with GPCRs other than rhodopsin. These findings suggest that GPCR signaling may be differentially regulated depending on the cellular complement of arrestin isoforms and the ability of arrestins to interact with other cellular proteins.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 20/09/20 alle ore 04:44:09