ArticleMolecular and cellular biology2008
Two adjacent docking sites in the yeast Hog1 mitogen-activated protein (MAP) kinase differentially interact with the Pbs2 MAP kinase kinase and the Ptp2 protein tyrosine phosphatase.
Article in Molecular and cellular biology, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 35 papers.
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35 citing papers in PubMed, 60 citations in OpenAlex.
- Article
- Acetic acid-induced stress granules function as scaffolding complexes for Hog1 activation by Pbs2.The Journal of cell biology · 2025Article
- Efficient genes identification via quantitative trait loci analysis by crossbreeding of sake and laboratory yeast.Applied microbiology and biotechnology · 2025Article
- Engineering transcriptional regulatory networks for improving second-generation fuel ethanol production inSynthetic and systems biotechnology · 2025Review
- Positive feedback induces switch between distributive and processive phosphorylation of Hog1.Nature communications · 2023Article
- Host- and virus-induced gene silencing of HOG1-MAPK cascade genes in Rhizophagus irregularis inhibit arbuscule development and reduce resistance of plants to drought stress.Plant biotechnology journal · 2023Article
- The yeast two-component SLN1 branch of the HOG pathway and the scaffolding activity of Pbs2 modulate the response to endoplasmic reticulum stress induced by tunicamycin.International microbiology : the official journal of the Spanish Society for Microbiology · 2022Article
- Molecular cloning and sequence analysis of a mitogen-activated protein kinase gene in the Antarctic yeast Rhodotorula mucilaginosa AN5.Molecular biology reports · 2021Article
- A self-balancing circuit centered on MoOsm1 kinase governs adaptive responses to host-derived ROS ineLife · 2020Article
- Protein Homeostasis Networks and the Use of Yeast to Guide Interventions in Alzheimer's Disease.International journal of molecular sciences · 2020Review
- Article
- Negative feedback-loop mechanisms regulating HOG- and pheromone-MAPK signaling in yeast.Current genetics · 2020Review
- The High Osmolarity Glycerol (HOG) Pathway Functions in Osmosensing, Trap Morphogenesis and Conidiation of the Nematode-Trapping FungusJournal of fungi (Basel, Switzerland) · 2020Article
- The High Osmolarity Glycerol Mitogen-Activated Protein Kinase regulates glucose catabolite repression in filamentous fungi.PLoS genetics · 2020Article
- Osmostress enhances activating phosphorylation of Hog1 MAP kinase by mono-phosphorylated Pbs2 MAP2K.The EMBO journal · 2020Article
- A phosphorylated transcription factor regulates sterol biosynthesis in Fusarium graminearum.Nature communications · 2019Article
- Article
- Hog1 Regulates Stress Tolerance and Virulence in the Emerging Fungal Pathogen Candida auris.mSphere · 2018Article
- Intracellular mechanism by which arsenite activates the yeast stress MAPK Hog1.Molecular biology of the cell · 2018Article
- The phosphorelay signal transduction system in Candida glabrata: an in silico analysis.Journal of molecular modeling · 2017Article
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Functional interactions between a mitogen-activated protein kinase (MAPK) and its regulators require specific docking interactions. Here, we investigated the mechanism by which the yeast osmoregulatory Hog1 MAPK specifically interacts with its activator, the MAPK kinase Pbs2, and its major inactivator, the protein phosphatase Ptp2. We found, in the N-terminal noncatalytic region of Pbs2, a specific Hog1-binding domain, termed HBD-1. We also defined two adjacent Pbs2-binding sites in Hog1, namely, the common docking (CD) domain and Pbs2-binding domain 2 (PBD-2). The PBD-2 docking site appears to be sterically blocked in the intact Hog1 molecule, but its affinity to Pbs2 is apparent in shorter fragments of Hog1. Both the CD and the PBD-2 docking sites are required for the optimal activation of Hog1 by Pbs2, and in the absence of both sites, Hog1 cannot be activated by Pbs2. These data suggest that the initial interaction of Pbs2 with the CD site might induce a conformational change in Hog1 so that the PBD-2 site becomes accessible. The CD and PBD-2 docking sites are also involved in the specific interaction between Hog1 and Ptp2 and govern the dynamic dephosphorylation of activated Hog1. Thus, the CD and the PBD-2 docking sites play critical roles in both the activation and inactivation of Hog1.
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