Mutational analysis suggests that activation of the yeast pheromone response mitogen-activated protein kinase pathway involves conformational changes in the Ste5 scaffold protein.

@article{Sette2000MutationalAS,
  title={Mutational analysis suggests that activation of the yeast pheromone response mitogen-activated protein kinase pathway involves conformational changes in the Ste5 scaffold protein.},
  author={Claudio Sette and C J Inouye and Shannon L. Stroschein and Phillip J. Iaquinta and J. Thorner},
  journal={Molecular biology of the cell},
  year={2000},
  volume={11 11},
  pages={
          4033-49
        }
}
Ste5 is essential for pheromone response and binds components of a mitogen-activated protein kinase (MAPK) cascade: Ste11 (MEKK), Ste7 (MEK), and Fus3 (MAPK). Pheromone stimulation releases Gbetagamma (Ste4-Ste18), which recruits Ste5 and Ste20 (p21-activated kinase) to the plasma membrane, activating the MAPK cascade. A RING-H2 domain in Ste5 (residues 177-229) negatively regulates Ste5 function and mediates its interaction with Gbetagamma. Ste5(C177A C180A), carrying a mutated RING-H2 domain… CONTINUE READING

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A Laboratory Course Manual for Methods in Yeast Genetics

  • F. Sherman, G. R. Fink, J. B. Hicks
  • Cold Spring Harbor,
  • 1986
Highly Influential
3 Excerpts

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