A G protein γ subunit-like domain shared between RGS11 and other RGS proteins specifies binding to Gβ5 subunits

B. E. Snow, A. M. Krumins, G. M. Brothers, S. F. Lee, M. A. Wall, S. Chung, J. Mangion, S. Arya, A. G. Gilman, D. P. Siderovski

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233 Scopus citations

Abstract

Regulators of G protein signaling (RGS) proteins act as GTPase-activating proteins (GAPs) toward the α subunits of heterotrimeric, signal-transducing G proteins. RGS11 contains a G protein γ subunit-like (GGL) domain between its Dishevelled/Egl-10/Pleckstrin and RGS domains. GGL domains are also found in RGS6, RGS7, RGS9, and the Caenorhabditis elegans protein EGL-10. Coexpression of RGS11 with different Gβ subunits reveals specific interaction between RGS11 and Gβ5. The expression of mRNA for RGS11 and Gβ5 in human tissues overlaps. The Gβ5/RGS11 heterodimer acts as a GAP on Gαo, apparently selectively. RGS proteins that contain GGL domains appear to act as GAPs for Gα proteins and form complexes with specific Gβ subunits, adding to the combinatorial complexity of G protein-mediated signaling pathways.

Original languageEnglish (US)
Pages (from-to)13307-13312
Number of pages6
JournalProceedings of the National Academy of Sciences of the United States of America
Volume95
Issue number22
DOIs
StatePublished - Oct 27 1998

ASJC Scopus subject areas

  • General

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