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

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Marcus, S, Polverino, A, Barr, M, Wigler, M·1994·Proceedings of the National Academy of Sciences

Abstract

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.

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Metadata

Authors
Marcus, S., Polverino, A., Barr, M., & Wigler, M.
Venue
Proceedings of the National Academy of Sciences
Published
1994-08-02
Volume
91
Issue
16
Pages
7762-7766
ISSN
  • 0027-8424 (ISSN-L)
  • 1091-6490
OpenAlex
W2069883690
Cited by
242
References
0
FWCI
8.46
Type
journal article
Language
en
Open access
green

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CoChat. (2026). Citation check: Complexes between STE5 and components of the pheromone-responsive mitogen-activated protein kinase module. https://app.cochat.ai/papers/10.1073/pnas.91.16.7762
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Marcus, S., Polverino, A., Barr, M., & Wigler, M. (1994). Complexes between STE5 and components of the pheromone-responsive mitogen-activated protein kinase module. Proceedings of the National Academy of Sciences. https://doi.org/10.1073/pnas.91.16.7762

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