ArticleNature communications2023
Positive feedback induces switch between distributive and processive phosphorylation of Hog1.
Article in Nature communications, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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Who cites it
7 citing papers in PubMed.
- HOG Signaling: A Multifunctional Regulator of Stress Homeostasis inJournal of fungi (Basel, Switzerland) · 2026Review
- PEtab Select: Specification standard and supporting software for automated model selection.PLoS computational biology · 2026Article
- Enzymatic DNA Reaction Networks for Orchestrating Stimuli-Dependent Temporal Molecular Pulse.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026Article
- Jaxkineticmodel: Neural ordinary differential equations inspired parameterization of kinetic models.PLoS computational biology · 2025Article
- KINAID: an orthology-based kinase-substrate prediction and analysis tool for phosphoproteomics.Bioinformatics (Oxford, England) · 2025Article
- Engineering transcriptional regulatory networks for improving second-generation fuel ethanol production inSynthetic and systems biotechnology · 2025Review
- Shared and redundant proteins coordinate signal cross-talk between MAPK pathways in yeast.Molecular biology of the cell · 2024Article
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Authors and funding
9 authors.
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Abstract
Cellular decision making often builds on ultrasensitive MAPK pathways. The phosphorylation mechanism of MAP kinase has so far been described as either distributive or processive, with distributive mechanisms generating ultrasensitivity in theoretical analyses. However, the in vivo mechanism of MAP kinase phosphorylation and its activation dynamics remain unclear. Here, we characterize the regulation of the MAP kinase Hog1 in Saccharomyces cerevisiae via topologically different ODE models, parameterized on multimodal activation data. Interestingly, our best fitting model switches between distributive and processive phosphorylation behavior regulated via a positive feedback loop composed of an affinity and a catalytic component targeting the MAP kinase-kinase Pbs2. Indeed, we show that Hog1 directly phosphorylates Pbs2 on serine 248 (S248), that cells expressing a non-phosphorylatable (S248A) or phosphomimetic (S248E) mutant show behavior that is consistent with simulations of disrupted or constitutively active affinity feedback and that Pbs2-S248E shows significantly increased affinity to Hog1 in vitro. Simulations further suggest that this mixed Hog1 activation mechanism is required for full sensitivity to stimuli and to ensure robustness to different perturbations.
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