Gγ-like (GGL) domains: New frontiers in G-protein signaling and β-propeller scaffolding

John Sondek, David P. Siderovski

Research output: Contribution to journalArticle

104 Scopus citations

Abstract

The standard model of signal transduction from G-protein-coupled receptors (GPCRs) involves guanine nucleotide cycling by a heterotrimeric G-protein assembly composed of Gα, Gβ, and Gγ subunits. The WD-repeat β-propeller protein Gβ and the alpha-helical, isoprenylated polypeptide Gγ are considered obligate dimerization partners; moreover, conventional Gβγ heterodimers are considered essential to the functional coupling of Gα subunits to receptors. However, our recent discovery of a Gβ5 binding site (the Gγ-like or "GGL" domain) within several regulators of G-protein signaling (RGS) proteins revealed the potential for functional GPCR/Gα coupling in the absence of a conventional Gγ subunit. In addition, we posit that the interaction between Gβ5 isoforms and the GGL domains of RGS proteins represents a general mode of binding between β-propeller proteins and their partners, extending beyond the realm of G-protein-linked signal transduction.

Original languageEnglish
Pages (from-to)1329-1337
Number of pages9
JournalBiochemical Pharmacology
Volume61
Issue number11
DOIs
StatePublished - 1 Jun 2001

Keywords

  • G-gamma-like (GGL) domain
  • Guanine nucleotide-binding protein (G protein)
  • Kinesin
  • PDE4D5
  • RACK1
  • Regulators of G-protein signaling (RGS) proteins

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