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RGS7 Attenuates Signal Transduction Through the G αq Family of Heterotrimeric G Proteins in Mammalian Cells
Author(s) -
Shuey David J.,
Betty Maria,
Jones Philip G.,
Khawaja Xavier Z.,
Cockett Mark I.
Publication year - 1998
Publication title -
journal of neurochemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.75
H-Index - 229
eISSN - 1471-4159
pISSN - 0022-3042
DOI - 10.1046/j.1471-4159.1998.70051964.x
Subject(s) - heterotrimeric g protein , gtpase activating protein , g protein , microbiology and biotechnology , biology , gq alpha subunit , gtp binding protein regulators , gtpase , signal transduction , g beta gamma complex
The RGS proteins are a recently discovered family of G protein regulators that have been shown to act as GTPase‐activating proteins (GAPs) on the G αi and G αq subfamilies of the heterotrimeric G proteins. Here, we demonstrate that RGS7 is a potent GAP in vitro on G αi1 and G αo heterotrimeric proteins and that RGS7 acts to down‐regulate G αq ‐mediated calcium mobilization in a whole‐cell assay system using a transient expression protocol. This RGS protein and RGS4 are reported to be expressed predominantly in brain, and in situ hybridization studies have revealed similarities in the regional distribution of RGS and G αq mRNA expression. Our findings provide further evidence to support a functional role for RGS4 and RGS7 in G αq ‐mediated signaling in the CNS.