title: Cellular noise suppression by the regulator of G protein signaling Sst2.
abstract: G proteins and their associated receptors process information from a variety of environmental stimuli to induce appropriate cellular responses. Generally speaking, each cell in a population responds within defined limits, despite large variation in the expression of protein signaling components. Therefore, we postulated that noise suppression is encoded within the signaling system. Using the yeast mating pathway as a model, we evaluated the ability of a regulator of G protein signaling (RGS) protein to suppress noise. We found that the RGS protein Sst2 limits variability in transcription and morphogenesis in response to pheromone stimulation. While signal suppression is a result of both the GAP (GTPase accelerating) and receptor binding functions of Sst2, noise suppression requires only the GAP activity. Taken together, our findings reveal a hitherto overlooked role of RGS proteins as noise suppressors and demonstrate an ability to uncouple signal and noise in a prototypical stimulus-response pathway.
authors: Department of Biochemistry and Biophysics, University of North Carolina at Chapel Hill, Chapel Hill, NC 27599, USA.
authors: Gauri
authors: G
authors: Dixit
authors: Department of Biochemistry and Biophysics, University of North Carolina at Chapel Hill, Chapel Hill, NC 27599, USA; Department of Pharmacology, University of North Carolina at Chapel Hill, Chapel Hill, NC 27599, USA.
authors: Joshua B
authors: JB
authors: Kelley
authors: Department of Pharmacology, University of North Carolina at Chapel Hill, Chapel Hill, NC 27599, USA.
authors: John R
authors: JR
authors: Houser
authors: Department of Pharmacology, University of North Carolina at Chapel Hill, Chapel Hill, NC 27599, USA.
authors: Timothy C
authors: TC
authors: Elston
authors: Department of Biochemistry and Biophysics, University of North Carolina at Chapel Hill, Chapel Hill, NC 27599, USA; Department of Pharmacology, University of North Carolina at Chapel Hill, Chapel Hill, NC 27599, USA. Electronic address: hdohlman@med.unc.edu.
authors: Henrik G
authors: HG
authors: Dohlman
mesh_terms: D016764:Cell Polarity; D019204:GTP-Binding Proteins / Q000378:metabolism*; D020690:GTPase-Activating Proteins / Q000502:physiology*; D010675:Pheromones / Q000378:metabolism; D029701:Saccharomyces cerevisiae Proteins / Q000502:physiology*; D015398:Signal Transduction; D014158:Transcription, Genetic; D020846:cdc42 GTP-Binding Protein, Saccharomyces cerevisiae / Q000378:metabolism; D020710:RGS Proteins
chemical_list: D019204:GTP-Binding Proteins; D020690:GTPase-Activating Proteins; D010675:Pheromones; D029701:Saccharomyces cerevisiae Proteins; D020846:cdc42 GTP-Binding Protein, Saccharomyces cerevisiae; C094301:SST2 protein, S cerevisiae; D020710:RGS Proteins