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={C. Sette and C. Inouye and S. L. Stroschein and P. J. Iaquinta and J. Thorner},
  journal={Molecular biology of the cell},
  year={2000},
  volume={11 11},
  pages={
          4033-49
        }
}
  • C. Sette, C. Inouye, +2 authors J. Thorner
  • Published 2000
  • Medicine, Biology
  • Molecular biology of the cell
  • 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
    Pheromone response, mating and cell biology.
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    The Ste5p scaffold.
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    Cdc42 Regulation of Kinase Activity and Signaling by the Yeast p21-Activated Kinase Ste20
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    Function of the MAPK scaffold protein, Ste5, requires a cryptic PH domain.
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