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Curr Biol. 2005 Oct 25;15(20):R843-54.

New roles for Galpha and RGS proteins: communication continues despite pulling sisters apart.

Author information

1
Department of Pharmacology, UT Southwestern Medical Center, Dallas, TX 75390, USA. thomas.wilke@utsouthwestern.edu

Abstract

Large G protein alpha 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 Galpha 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 Galpha 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.

PMID:
16243026
DOI:
10.1016/j.cub.2005.10.008
[Indexed for MEDLINE]
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