Ste5 RING-H2 domain: role in Ste4-promoted oligomerization for yeast pheromone signaling.

@article{Inouye1997Ste5RD,
  title={Ste5 RING-H2 domain: role in Ste4-promoted oligomerization for yeast pheromone signaling.},
  author={Carla Inouye and N. P. S. Dhillon and J. Thorner},
  journal={Science},
  year={1997},
  volume={278 5335},
  pages={
          103-6
        }
}
Ste5 is a scaffold for the mitogen-activated protein kinase (MAPK) cascade components in a yeast pheromone response pathway. Ste5 also associates with Ste4, the beta subunit of a heterotrimeric guanine nucleotide-binding protein, potentially linking receptor activation to stimulation of the MAPK cascade. A RING-H2 motif at the Ste5 amino terminus is apparently essential for function because Ste5(C177S) and Ste5(C177A C180A) mutants did not rescue the mating defect of a ste5Delta cell. In vitro… CONTINUE READING
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