RGS domain-independent Sst2 action
by Shanks, Ryan, M.S., THE UNIVERSITY OF NORTH CAROLINA AT CHAPEL HILL, 2008, 30 pages; 1454958

Abstract:

RGS proteins are a family of proteins that share a conserved RGS domain that contacts Gα to accelerate GTP hydrolysis. It is thought that the function of RGS proteins lies not only in the RGS domain, but also through interactions mediated by domains outside of this region. Other than its RGS domain, the yeast RGS protein Sst2 contains two DEP domains. It has been shown that the DEP domains of Sst2 facilitate binding between Sst2 and the GPCR Ste2. The presumed function of this binding is to target Sst2 GAP activity towards the mating pathway Ga. Here, we show an additional function of the DEP domains of Sst2 that is independent of GAP activity. Expression of only the N-terminal DEP domains of Sst2 dampens the mating response. We present preliminary data testing two potential mechanisms of this action, and conclude with a discussion of the future directions of this work.

 
AdvisersHenrik Dohlman; David Siderovski
SchoolTHE UNIVERSITY OF NORTH CAROLINA AT CHAPEL HILL
SourceMAI/ 46-06, p. , Aug 2008
Source TypeThesis
SubjectsPharmacology
Publication Number1454958
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