A novel kind of G protein heterodimer: The Gβ5-RGS complex

D. Scott Witherow, Vladlen Z. Slepak

Research output: Contribution to journalReview article

37 Scopus citations

Abstract

The fifth member of the G protein β the subunit family, G,β5, has been shown to bind exclusively to a subfamily of regulators of G protein signaling (RGS) including RGS6, RGS7, RGS9, and RGS11. This interaction occurs through a G protein gamma-like (GGL) domain present in members of this RGS subfamily and is the only reported instance in which a Gβ subunit is not bound to a G-γ subunit. The Gβ5-RGS interaction has been demonstrated both in vitro and in vivo and has been shown to stabilize the dimer against proteolytic degradation. GTPase activating protein (GAP) assays suggest that Gβ5-RGS7 acts specifically on Gαq, however in cell-based assays it also inhibited Gαi- and Gαq-mediated signaling. The role of the dimer in signaling and the function of Qα5 moiety within the complex are poorly understood. This review summarizes the information about the assembly and funntion of Gβ5-RGS dimers, as well as their posttranslational modifications and localization.

Original languageEnglish (US)
Pages (from-to)205-212
Number of pages8
JournalReceptors and Channels
Volume9
Issue number3
DOIs
StatePublished - Jul 29 2003

Keywords

  • Bioinformatics
  • Gβ5
  • GAF
  • GGL
  • Protein purification
  • RGS

ASJC Scopus subject areas

  • Clinical Biochemistry
  • Endocrinology
  • Cell Biology

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