A conserved protein interaction network involving the yeast MAP kinases Fus3 and Kss1
Open accessAbstract
The Saccharomyces cerevisiae mitogen-activated protein kinases (MAPKs) Fus3 and Kss1 bind to multiple regulators and substrates. We show that mutations in a conserved docking site in these MAPKs (the CD/7m region) disrupt binding to an important subset of their binding partners, including the Ste7 MAPK kinase, the Ste5 adaptor/scaffold protein, and the Dig1 and Dig2 transcriptional repressors. Supporting the possibility that Ste5 and Ste7 bind to the same region of the MAPKs, they partially competed for Fus3 binding. In vivo, some of the MAPK mutants displayed reduced Ste7-dependent phosphorylation, and all of them exhibited multiple defects in mating and pheromone response. The Kss1 mutants were also defective in Kss1-imposed repression of Ste12. We conclude that MAPKs contain a structurally and functionally conserved docking site that mediates an overall positively acting network of interactions with cognate docking sites on their regulators and substrates. Key features of this interaction network appear to have been conserved from yeast to humans.
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The structural and biochemical analysis, together with other studies, clarified the minimal sequence requirements for linear motifs to bind the MAPK docking groove.
“Our structural and biochemical analysis in combination with other studies clarified the minimal sequence requirements for linear motifs to bind the MAPK docking groove (42-47).”
From Specificity of Linear Motifs That Bind to a Common Mitogen-Activated Protein Kinase Docking Groove (2012) · cites this paper as [47]
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References 38 · Cited by 81
- Authors
- Kusari, A. B., Molina, D. M., Sabbagh, W., Lau, C. S., & Bardwell, L.
- Affiliations
- University of California, Irvine (US)
- Corresponding author
- Bardwell, Lee
- ORCID
- Bardwell, Lee
- Venue
- The Journal of Cell Biology
- Publisher
- Rockefeller University Press
- Published
- 2004-01-19
- Volume
- 164
- Issue
- 2
- Pages
- 267-277
- ISSN
- 0021-9525 (ISSN-L)
- 1540-8140
- PMC
- PMC2172336
- OpenAlex
- W2115197624
- Cited by
- 81
- References
- 38
- Citations by year
- 2026: 1 · 2025: 1 · 2023: 2 · 2020: 2 · 2019: 5 · 2018: 2 · 2017: 3 · 2016: 2 · 2015: 4 · 2014: 2 · 2012: 6
- FWCI
- 4.15
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Licence
- cc-by-nc-sa
- Locations
- The Journal of Cell Biology (publishedVersion)
- Europe PMC (PubMed Central) (publishedVersion, cc-by-nc-sa)
- PubMed Central (publishedVersion, cc-by-nc-sa)
- PubMed (publishedVersion)
- eScholarship (California Digital Library) (submittedVersion)
- Funders
- National Institute of General Medical Sciences (GM-60366, R33GM069013, R01GM060366, GM69013, R21GM069013)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Fungal and yeast genetics research
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Kinase Regulation and GTPase Signaling
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Tyrosine Phosphatases
- Keywords
- FUS3, Kss1, protein-protein interaction, mating response, pheromone response, Saccharomyces cerevisiae
- MeSH terms
- Amino Acid Sequence, Binding Sites, Carrier Proteins, Homeostasis, Molecular Sequence Data, Protein Kinases, Recombinant Proteins, Saccharomyces cerevisiae, Mutagenesis, Site-Directed, Mitogen-Activated Protein Kinases, Mitogen-Activated Protein Kinase Kinases, Saccharomyces cerevisiae Proteins, Adaptor Proteins, Signal Transducing
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