GAIP and RGS4 are GTPase-activating proteins for the G(i) subfamily of G protein α subunits

David M. Berman, Thomas M. Wilkie, Alfred G. Gilman

Research output: Contribution to journalArticle

615 Citations (Scopus)

Abstract

A novel class of regulators of G protein signaling (RGS) proteins has been identified recently. Genetic evidence suggests that RGS proteins inhibit G protein-mediated signaling at the level of the receptor-G protein interaction or the G protein α subunit itself. We have found that two RGS family members, GAIP and RGS4, are GTPase-activating proteins (GAPs), accelerating the rate of GTP hydrolysis by G(iα1) at least 40-fold. All G(i) subfamily members assayed were substrates for these GAPs; G(sα) was not. RGS4 activates the GTPase activity of certain G(iα1) mutants (e.g., R178C), but not others (e.g., Q204L). The GAP activity of RGS proteins is consistent with their proposed role as negative regulators of G protein-mediated signaling.

Original languageEnglish (US)
Pages (from-to)445-452
Number of pages8
JournalCell
Volume86
Issue number3
DOIs
StatePublished - Aug 9 1996

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RGS Proteins
GTPase-Activating Proteins
Protein Subunits
GTP-Binding Proteins
GTP-Binding Protein Regulators
GTP Phosphohydrolases
Guanosine Triphosphate
Hydrolysis
Substrates

ASJC Scopus subject areas

  • Cell Biology
  • Molecular Biology

Cite this

GAIP and RGS4 are GTPase-activating proteins for the G(i) subfamily of G protein α subunits. / Berman, David M.; Wilkie, Thomas M.; Gilman, Alfred G.

In: Cell, Vol. 86, No. 3, 09.08.1996, p. 445-452.

Research output: Contribution to journalArticle

Berman, David M. ; Wilkie, Thomas M. ; Gilman, Alfred G. / GAIP and RGS4 are GTPase-activating proteins for the G(i) subfamily of G protein α subunits. In: Cell. 1996 ; Vol. 86, No. 3. pp. 445-452.
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