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Trends Pharmacol Sci. 1999 Sep;20(9):376-82.

Emerging roles for RGS proteins in cell signalling.

Author information

1
Department of Pharmacology, Emory University School of Medicine, 5009 Rollins Research Center, 1510 Clifton Road, Atlanta, GA 30322-3090, USA. jhepler@emory.edu

Abstract

Regulators of G-protein signalling (RGS proteins) are a family of highly diverse, multifunctional signalling proteins that share a conserved 120 amino acid domain (RGS domain). RGS domains bind directly to activated Galpha subunits and act as GTPase-activating proteins (GAPs) to attenuate and/or modulate hormone and neurotransmitter receptor-initiated signalling by both Galpha-GTP and Gbetagamma. Apart from this structural domain, which is shared by all known RGS proteins, these proteins differ widely in their overall size and amino acid identity and possess a remarkable variety of structural domains and motifs. These biochemical features impart signalling functions and/or enable RGS proteins to interact with a growing list of unexpected protein-binding partners with diverse cellular roles. New appreciation for the broader cellular functions of RGS proteins challenges established models of G-protein signalling and serves to identify these proteins as central participants in receptor signalling and cell physiology.

PMID:
10462761
DOI:
10.1016/s0165-6147(99)01369-3
[Indexed for MEDLINE]

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