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Titolo:
RGS2 G0S8 IS A SELECTIVE INHIBITOR OF GQ-ALPHA FUNCTION/
Autore:
HEXIMER SP; WATSON N; LINDER ME; BLUMER KJ; HEPLER JR;
Indirizzi:
EMORY UNIV,SCH MED,DEPT PHARMACOL,ROLLINS RES CTR 5009,1510 CLIFTON RD ATLANTA GA 30329 EMORY UNIV,SCH MED,DEPT PHARMACOL,ROLLINS RES CTR 5009 ATLANTA GA 30329 WASHINGTON UNIV,SCH MED,DEPT CELL BIOL & PHYSIOL ST LOUIS MO 63110
Titolo Testata:
Proceedings of the National Academy of Sciences of the United Statesof America
fascicolo: 26, volume: 94, anno: 1997,
pagine: 14389 - 14393
SICI:
0027-8424(1997)94:26<14389:RGIASI>2.0.ZU;2-I
Fonte:
ISI
Lingua:
ENG
Soggetto:
GTPASE-ACTIVATING PROTEINS; SF9 CELLS; SUBUNITS; PURIFICATION; REGULATOR; FAMILY; RGS4;
Keywords:
REGULATOR OF G PROTEIN SIGNALING; PHOSPHOINOSITIDE HYDROLYSIS; PHOSPHOLIPASE C-BETA;
Tipo documento:
Article
Natura:
Periodico
Citazioni:
25
Recensione:
Indirizzi per estratti:
Citazione:
S.P. Heximer et al., "RGS2 G0S8 IS A SELECTIVE INHIBITOR OF GQ-ALPHA FUNCTION/", Proceedings of the National Academy of Sciences of the United Statesof America, 94(26), 1997, pp. 14389-14393

Abstract

RGS (regulators of G protein signaling) proteins are GTPase activating proteins that inhibit signaling by heterotrimeric G proteins. All RGS proteins studied to date act on members of the Gi alpha family, but not Gs alpha or G12 alpha. RGS4 regulates Gi alpha family members and Gq alpha. RGS2 (G0S8) is exceptional because the G proteins it regulates have not been identified. We report that RGS2 is a selective and potent inhibitor of Gq alpha function. RGS2 selectively binds Gq alpha, but not other G alpha proteins (Gi, Go, Gs, G12/13) in brain membranes; RGS4 binds Gq alpha and Gi alpha family members. RGS2 binds purifiedrecombinant Gq alpha, but not Go alpha, whereas RGS4 binds either. RGS2 does not stimulate the GTPase activities of Gs alpha or Gi alpha family members, even at a protein concentration 3000-fold higher than issufficient to observe effects of RGS4 on Gi alpha family members. In contrast, RGS2 and RGS4 completely inhibit Gq-directed activation of phospholipase C in cell membranes. When reconstituted with phospholipidvesicles, RGS2 is 10-fold more potent than RGS4 in blocking Gq alpha-directed activation of phospholipase C beta 1. These results identify a clear physiological role for RGS2, and describe the first example ofan RGS protein that is a selective inhibitor of Gq alpha function.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 24/01/21 alle ore 01:45:04