Complexes between STE5 and components of the pheromone-responsive mitogen-activated protein kinase module.

We present genetic evidence for complex formation of STE5 and the STE11, STE7, and FUS3 protein kinases, the pheromone-responsive mitogen-activated protein kinase module of Saccharomyces cerevisiae. Interaction between STE5 and STE11 is not dependent on STE7, and interaction between STE5 and STE7 does not require STE11. The N-terminal regulatory domain ...
of STE11 is both necessary and sufficient for interaction with STE5. Interaction between STE7 and STE11 is bridged by STE5, suggesting the formation of a multiprotein complex. We also demonstrate biochemical interaction between STE5 and STE11 by using a combination of bacterially expressed fusion proteins and extracts prepared from yeast. Our results suggest that STE5 is a scaffolding protein that facilitates interactions between components of the pheromone-responsive mitogen-activated protein kinase module. We further propose that such scaffolding proteins serve to inhibit cross-talk between functionally unrelated mitogen-activated protein kinase modules within the same cell.
Mesh Terms:
Adaptor Proteins, Signal Transducing, Calcium-Calmodulin-Dependent Protein Kinases, Carrier Proteins, Fungal Proteins, MAP Kinase Kinase 1, MAP Kinase Kinase Kinases, Mitogen-Activated Protein Kinase Kinases, Mitogen-Activated Protein Kinases, Pheromones, Protein Kinases, Protein-Serine-Threonine Kinases, Protein-Tyrosine Kinases, Saccharomyces cerevisiae, Saccharomyces cerevisiae Proteins, Schizosaccharomyces pombe Proteins, Signal Transduction, Transcription Factors
Proc. Natl. Acad. Sci. U.S.A.
Date: Aug. 02, 1994
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