New roles for Gα and RGS proteins: Communication continues despite pulling sisters apart

Thomas M. Wilkie, Lisa Kinch

Research output: Contribution to journalReview article

57 Scopus citations

Abstract

Large G protein α subunits and their attendant regulators of G-protein signaling (RGS) proteins control both intercellular signaling and asymmetric cell divisions by distinct pathways. The classical pathway, found throughout higher eukaryotic organisms, mediates intercellular communication via hormone binding to G-protein-coupled receptors (GPCRs). Recent studies have led to the discovery of GPCR-independent activation of Gα subunits by the guanine nucleotide exchange factor RIC-8 in both asymmetric cell division and synaptic vesicle priming in metazoan organisms. Protein-protein interactions and protein function in each pathway are driven through the cycle of GTP binding and hydrolysis by the Gα subunit. This review builds a conceptual framework for understanding RIC-8-mediated pathways by comparison with the mechanism of classical G-protein activation and inhibition in GPCR signaling.

Original languageEnglish (US)
Pages (from-to)R843-R854
JournalCurrent Biology
Volume15
Issue number20
DOIs
StatePublished - Oct 25 2005

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ASJC Scopus subject areas

  • Biochemistry, Genetics and Molecular Biology(all)
  • Agricultural and Biological Sciences(all)

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