RGS proteins are a family of proteins that share a conserved RGS
domain that contacts Galpha 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.
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