Ras2 is a Saccharomyces cerevisiae guanine nucleotide-binding protein (encoded by the RAS2 gene) which becomes activated by binding GTP when glucose is present in the environment. It affects growth regulation and starvation response.
Ras2 becomes post-translationally modified in two ways, both being necessary for its activity: Upon activation, palmitoylation at its C terminus takes place and causes attachment from the cytoplasm to the plasma membrane. Farnesylation allows for efficient interaction with the downstream adenylate cyclase Cyr1p. In wild-type yeast deactivated Ras2 is transported to and degraded in the vacuole, a process for which Whi2 is essential. Disturbing this process leads to Ras2 accumulation at the mitochondrial membrane, a behavior that was not observed before.
Active Ras2 was also found in the nucleus, the reason is currently unknown.
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