RGS4 and GAIP are GTPase-activating proteins for G and block activation of phospholipase Cβ by γ-thio-GTP-G

J. R. Hepler, D. M. Berman, A. G. Gilman, T. Kozasa

Research output: Contribution to journalArticlepeer-review

326 Scopus citations

Abstract

RGS proteins constitute a newly appreciated and large group of negative regulators of G protein signaling. Four members of the RGS family act as GTPase-activating proteins (GAPs) with apparent specificity for members of the G subfamily of G protein subunits. We demonstrate here that two RGS proteins, RGS4 and GAIP, also act as GAPs for G, the Gα protein responsible for activation of phospholipase Cβ. Furthermore, these RGS proteins block activation of phospholipase Cβ by guanosine 5′-(3-O-thio)triphosphate-G. GAP activity does not explain this effect, which apparently results from occlusion of the binding site on Gα for effector. Inhibitory effects of RGS proteins on G protein-mediated signaling pathways can be demonstrated by simple mixture of RGS4 or GAIP with plasma membranes.

Original languageEnglish (US)
Pages (from-to)428-432
Number of pages5
JournalProceedings of the National Academy of Sciences of the United States of America
Volume94
Issue number2
DOIs
StatePublished - Jan 21 1997

ASJC Scopus subject areas

  • General

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