ArticleMolecular biology of the cell2015
Signal inhibition by a dynamically regulated pool of monophosphorylated MAPK.
Article in Molecular biology of the cell, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed, 24 citations in OpenAlex.
- Kinase KEY1 controls pyrenoid condensate size throughout the cell cycle by disrupting phase separation interactions.Nature cell biology · 2026Article
- Modulating p38 MAPK signaling by proteostasis mechanisms supports tissue integrity during growth and aging.Nature communications · 2023Article
- A walk-through MAPK structure and functionality with the 30-year-old yeast MAPK Slt2.International microbiology : the official journal of the Spanish Society for Microbiology · 2021Review
- Differential Role of Threonine and Tyrosine Phosphorylation in the Activation and Activity of the Yeast MAPK Slt2.International journal of molecular sciences · 2021Article
- Potassium starvation induces autophagy in yeast.The Journal of biological chemistry · 2020Article
- Systematic analysis of F-box proteins reveals a new branch of the yeast mating pathway.The Journal of biological chemistry · 2019Article
- Quantitative analysis of the yeast pheromone pathway.Yeast (Chichester, England) · 2019Article
- Mitogen-Activated Protein Kinase Phosphatases (MKPs) in Fungal Signaling: Conservation, Function, and Regulation.International journal of molecular sciences · 2019Review
- MAPK modulation of yeast pheromone signaling output and the role of phosphorylation sites in the scaffold protein Ste5.Molecular biology of the cell · 2019Article
- Spatio-temporal MAPK dynamics mediate cell behavior coordination during fungal somatic cell fusion.Journal of cell science · 2018Article
- Negative Feedback Phosphorylation of Gγ Subunit Ste18 and the Ste5 Scaffold Synergistically Regulates MAPK Activation in Yeast.Cell reports · 2018Article
- Analysis of the thresholds for transcriptional activation by the yeast MAP kinases Fus3 and Kss1.Molecular biology of the cell · 2018Article
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Authors and funding
6 authors at 1 institution in 1 country.
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Abstract
Protein kinases regulate a broad array of cellular processes and do so through the phosphorylation of one or more sites within a given substrate. Many protein kinases are themselves regulated through multisite phosphorylation, and the addition or removal of phosphates can occur in a sequential (processive) or a stepwise (distributive) manner. Here we measured the relative abundance of the monophosphorylated and dual-phosphorylated forms of Fus3, a member of the mitogen-activated protein kinase (MAPK) family in yeast. We found that upon activation with pheromone, a substantial proportion of Fus3 accumulates in the monophosphorylated state. Introduction of an additional copy of Fus3 lacking either phosphorylation site leads to dampened signaling. Conversely, cells lacking the dual-specificity phosphatase (msg5Δ) or that are deficient in docking to the MAPK-scaffold (Ste5(ND)) accumulate a greater proportion of dual-phosphorylated Fus3. The double mutant exhibits a synergistic, or "synthetic," supersensitivity to pheromone. Finally, we present a predictive computational model that combines MAPK scaffold and phosphatase activities and is sufficient to account for the observed MAPK profiles. These results indicate that the monophosphorylated and dual-phosphorylated forms of the MAPK act in opposition to one another. Moreover, they reveal a new mechanism by which the MAPK scaffold acts dynamically to regulate signaling.
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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.