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Complexes Between STE5 and Components of the Pheromone-Responsive Mitogen-Activated Protein Kinase Module
Stevan Marcus, Anthony Polverino, Maureen Barr and Michael Wigler
Proceedings of the National Academy of Sciences of the United States of America
Vol. 91, No. 16 (Aug. 2, 1994), pp. 7762-7766
Published by: National Academy of Sciences
Stable URL: http://www.jstor.org/stable/2365365
Page Count: 5
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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 mitogenactivated protein kinase modules within the same cell.
Proceedings of the National Academy of Sciences of the United States of America © 1994 National Academy of Sciences