ArticleCell2009
The Ste5 scaffold directs mating signaling by catalytically unlocking the Fus3 MAP kinase for activation.
Article in Cell, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 106 papers.
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Who cites it
106 citing papers in PubMed.
- A Virus-Inducible E3-RLCK-MADS Module Coordinates Suppression of Plant Immunity and Fertility in Rice.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026Article
- Phosphoregulation of the novel hemi-arrestin MAPK scaffold Sms1 prevents untimely mating.Nature communications · 2026Article
- Conserved and rewired MAPK networks in human fungal pathogens.FEMS yeast research · 2026Review
- TheIMA fungus · 2026Article
- Conserved signaling modules regulate filamentous growth in fungi: a model for eukaryotic cell differentiation.Genetics · 2024Review
- Signal transduction at GPCRs: Allosteric activation of the ERK MAPK by β-arrestin.Proceedings of the National Academy of Sciences of the United States of America · 2023Article
- Quantifying nonequilibrium dynamics and thermodynamics of cell fate decision making in yeast under pheromone induction.Biophysics reviews · 2023Article
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- Specificity models in MAPK cascade signaling.FEBS open bio · 2023Review
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- Chaperone-Dependent Degradation of Cdc42 Promotes Cell Polarity and Shields the Protein from Aggregation.Molecular and cellular biology · 2023Article
- Regulation of Cdc42 protein turnover modulates the filamentous growth MAPK pathway.The Journal of cell biology · 2022Article
- The Two Non-Visual Arrestins Engage ERK2 Differently.Journal of molecular biology · 2022Article
- Fus3, as a Critical Kinase in MAPK Cascade, Regulates Aflatoxin Biosynthesis by Controlling the Substrate Supply in Aspergillus flavus, Rather than the Cluster Genes Modulation.Microbiology spectrum · 2022Article
- Correlation Between Improved Mating Efficiency and Weakened Scaffold-Kinase Interaction in the Mating Pheromone Response Pathway Revealed by Interspecies Complementation.Frontiers in microbiology · 2022Article
- Cdc42-Specific GTPase-Activating Protein Rga1 Squelches Crosstalk between the High-Osmolarity Glycerol (HOG) and Mating Pheromone Response MAPK Pathways.Biomolecules · 2021Article
- Signal-mediated localization of Candida albicans pheromone response pathway components.G3 (Bethesda, Md.) · 2021Article
- Identification of a key G-protein coupled receptor in mediating appressorium formation and fungal virulence against insects.Science China. Life sciences · 2021Article
- Quantitative Acetylomics Revealed Acetylation-Mediated Molecular Pathway Network Changes in Human Nonfunctional Pituitary Neuroendocrine Tumors.Frontiers in endocrinology · 2021Article
- Review
46 more citing papers are in PubMed but not listed here.
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5 authors.
Funding
Abstract
The scaffold protein Ste5 is required to properly direct signaling through the yeast mating pathway to the mitogen-activated protein kinase (MAPK), Fus3. Scaffolds are thought to function by tethering kinase and substrate in proximity. We find, however, that the previously identified Fus3-binding site on Ste5 is not required for signaling, suggesting an alternative mechanism controls Fus3's activation by the MAPKK Ste7. Reconstituting MAPK signaling in vitro, we find that Fus3 is an intrinsically poor substrate for Ste7, although the related filamentation MAPK, Kss1, is an excellent substrate. We identify and structurally characterize a domain in Ste5 that catalytically unlocks Fus3 for phosphorylation by Ste7. This domain selectively increases the k(cat) of Ste7-->Fus3 phosphorylation but has no effect on Ste7-->Kss1 phosphorylation. The dual requirement for both Ste7 and this Ste5 domain in Fus3 activation explains why Fus3 is selectively activated by the mating pathway and not by other pathways that also utilize Ste7.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.