Emerging roles for RGS proteins in cell signalling.
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.
Hepler
J R
JR
Department of Pharmacology, Emory University School of Medicine, 5009 Rollins Research Center, 1510 Clifton Road, Atlanta, GA 30322-3090, USA. jhepler@emory.edu
D000818:Animals; D019204:GTP-Binding Proteins / Q000737:chemistry / Q000502:physiology*; D006728:Hormones / Q000502:physiology; D006801:Humans; D018377:Neurotransmitter Agents / Q000502:physiology; D011506:Proteins / Q000502:physiology*; D020710:RGS Proteins; D011956:Receptors, Cell Surface / Q000187:drug effects; D015398:Signal Transduction
D006728:Hormones; D018377:Neurotransmitter Agents; D011506:Proteins; D020710:RGS Proteins; C106375:RGS12 protein, human; D011956:Receptors, Cell Surface; C105345:Rgs2 protein, mouse; D019204:GTP-Binding Proteins