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FEBS Lett

Title:		"The core domain of RGS16 retains G-protein binding and GAP activity in vitro, but is not functional in vivo"
Author(s):		Chen C; Lin SC;
Address:		"Regulatory Biology Laboratory, Institute of Molecular and Cell Biology, National University of Singapore, Singapore"
Journal Title:		FEBS Lett
Year:		1998
Volume:		422
Issue:		3
Page Number:		359 - 362
DOI:		10.1016/s0014-5793(98)00042-8
ISSN/ISBN:		0014-5793 (Print) 0014-5793 (Linking)
Abstract:		"The regulators of G-protein signaling (RGS) family members contain a conserved region, the RGS domain, and are GTPase-activating proteins for many members of G-protein alpha-subunits. We report here that the core domain of RGS16 is sufficient for in vitro biochemical functions as assayed by its G-protein binding affinity and its ability to stimulate GTP hydrolysis by G alpha(o) protein. RGS16 also requires, in addition to the RGS domain, the divergent N-terminus for its biological function in the attenuation of pheromone signaling in yeast, whereas its C-terminus region is dispensable. Together with other evidence, these data support the notion that RGS proteins interact with other cellular factors and may serve to link specific G-proteins to different downstream effectors in G-protein-mediated signaling pathways"
Keywords:		Binding Sites GTP-Binding Proteins/*metabolism GTPase-Activating Proteins Mutagenesis Pheromones/metabolism Protein Binding Proteins/genetics/*metabolism *RGS Proteins Saccharomyces cerevisiae;
Notes:		"MedlineChen, C Lin, S C eng Research Support, Non-U.S. Gov't England 1998/03/14 FEBS Lett. 1998 Feb 6; 422(3):359-62. doi: 10.1016/s0014-5793(98)00042-8"