PHOSPHOLIPASE C-BETA-1 IS A GTPASE-ACTIVATING PROTEIN FOR GQ/11, ITS PHYSIOLOGICAL REGULATOR

被引：356

作者：

BERSTEIN, G

BLANK, JL

JHON, DY

EXTON, JH

RHEE, SG

ROSS, EM

机构：

[1] VANDERBILT UNIV, MED CTR,SCH MED,HOWARD HUGHES MED INST, DEPT MOLEC PHYSIOL & BIOPHYS, NASHVILLE, TN 37232 USA

[2] NHLBI, BIOCHEM LAB, BETHESDA, MD 20892 USA

来源：

CELL | 1992年 / 70卷 / 03期

关键词：

D O I：

10.1016/0092-8674(92)90165-9

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

Purified M1 muscarinic cholinergic receptor and G(q/11) were coreconstituted in lipid vesicles. Addition of purified phospholipase C-beta-1 (PLC-beta-1) further stimulated the receptor-promoted steady-state GTPase activity of G(q/11) up to 20-fold. Stimulation depended upon receptor-mediated GTP-GDP exchange. Addition of PLC-beta-1 caused a rapid burst of hydrolysis of G(q/11)-bound GTP that was at least 50-fold faster than in its absence. Thus, PLC-beta-1 stimulates hydrolysis of G(q/11)-bound GTP and acts as a GTPase-activating protein (GAP) for its physiologic regulator, G(q/11). GTPase-stimulating activity was specific both for PLC-beta-1 and G(g/11). Such GAP activity by an effector coupled to a trimeric G protein can reconcile slow GTP hydrolysis by pure G proteins in vitro with fast physiologic deactivation of G protein-mediated signaling.

引用

页码：411 / 418

页数：8

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