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Biophys J

Title:		The effects of replacing Sst2 with the heterologous RGS4 on polarization and mating in yeast
Author(s):		Tanaka H; Yi TM;
Address:		"Department of Developmental and Cell Biology, University of California, Irvine, California, USA"
Journal Title:		Biophys J
Year:		2010
Volume:		99
Issue:		4
Page Number:		1007 - 1017
DOI:		10.1016/j.bpj.2010.04.078
ISSN/ISBN:		1542-0086 (Electronic) 0006-3495 (Print) 0006-3495 (Linking)
Abstract:		"RGS proteins stimulate the deactivation of heterotrimeric G-proteins. The yeast RGS protein Sst2 is regulated at both the transcriptional and posttranscriptional levels. We replaced the SST2 gene with the distantly related human RGS4 gene, which consists of the catalytic domain and an N-terminal membrane attachment peptide, and replaced the native promoter (P(SST2)) with the heterologous tetracycline-repressible promoter (P(TET)). We then measured the effect of the substitutions on pheromone sensitivity, mating, and polarization. Although the pheromone sensitivity was essentially normal, there were differences in mating and polarization. In particular, the RGS4-substituted strains did not form multiple mating projections at high levels of alpha-factor, but instead formed a single malformed projection, which frequently gave rise to a bud. We provide evidence that this phenotype arose because unlike Sst2, RGS4 did not localize to the projection. We use mathematical modeling to argue that localization of Sst2 to the projection prevents excess G-protein activation during the pheromone response. In addition, modeling and experiments demonstrate that the dose of Sst2 influences the frequency of mating projection formation"
Keywords:		"*Cell Polarity/drug effects GTP-Binding Proteins/metabolism GTPase-Activating Proteins/genetics/*metabolism Gene Expression Regulation, Fungal/drug effects Humans Models, Biological Mutant Proteins/metabolism Phenotype Pheromones/pharmacology Promoter Reg;"
Notes:		"MedlineTanaka, Hiromasa Yi, Tau-Mu eng P50 GM076516/GM/NIGMS NIH HHS/ R01 GM075309/GM/NIGMS NIH HHS/ R01GM75309/GM/NIGMS NIH HHS/ P50GM76516/GM/NIGMS NIH HHS/ Research Support, N.I.H., Extramural 2010/08/18 Biophys J. 2010 Aug 9; 99(4):1007-17. doi: 10.1016/j.bpj.2010.04.078"