ArticleMolecular and cellular biology2008
Phosphorylated Ssk1 prevents unphosphorylated Ssk1 from activating the Ssk2 mitogen-activated protein kinase kinase kinase in the yeast high-osmolarity glycerol osmoregulatory pathway.
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 47 papers.
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Who cites it
47 citing papers in PubMed, 60 citations in OpenAlex.
- Article
- Hybrid histidine kinases shape the architecture of the high osmolarity glycerol (HOG) pathway: from Saccharomyces cerevisiae to the priority pathogen Aspergillus fumigatus and other filamentous fungi.FEMS microbiology reviews · 2026Review
- Engineering a xylose fermenting yeast for lignocellulosic ethanol production.Nature chemical biology · 2025Article
- The relationship mammalian p38 with human health and its homolog Hog1 in response to environmental stresses inFrontiers in cell and developmental biology · 2025Review
- Osmotic Stress Responses, Cell Wall Integrity, and Conidiation Are Regulated by a Histidine Kinase Sensor inJournal of fungi (Basel, Switzerland) · 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
- AoSsk1, a Response Regulator Required for Mycelial Growth and Development, Stress Responses, Trap Formation, and the Secondary Metabolism inJournal of fungi (Basel, Switzerland) · 2022Article
- Histidine kinase two-component response regulators Ssk1, Skn7 and Rim15 differentially control growth, developmental and volatile organic compounds emissions as stress responses in Trichoderma atroviride.Current research in microbial sciences · 2022Article
- Inhibitory effect of berberine hydrochloride against Candida albicans and the role of the HOG-MAPK pathway.The Journal of antibiotics · 2021Article
- Predicted Functional and Structural Diversity of Receiver Domains in Fungal Two-Component Regulatory Systems.mSphere · 2021Article
- Histidine Kinase Sln1 and cAMP/PKA Signaling Pathways Antagonistically RegulateJournal of fungi (Basel, Switzerland) · 2021Article
- An engineered protein-phosphorylation toggle network with implications for endogenous network discovery.Science (New York, N.Y.) · 2021Article
- Ypd1 Is an Essential Protein of the Major Fungal PathogenFrontiers in fungal biology · 2021Article
- Negative feedback-loop mechanisms regulating HOG- and pheromone-MAPK signaling in yeast.Current genetics · 2020Review
- Osmostress enhances activating phosphorylation of Hog1 MAP kinase by mono-phosphorylated Pbs2 MAP2K.The EMBO journal · 2020Article
- Insights revealed by the co-crystal structure of the Saccharomyces cerevisiae histidine phosphotransfer protein Ypd1 and the receiver domain of its downstream response regulator Ssk1.Protein science : a publication of the Protein Society · 2019Article
- Phenylpyrrole fungicides act on triosephosphate isomerase to induce methylglyoxal stress and alter hybrid histidine kinase activity.Scientific reports · 2019Article
- Article
- Membrane Thickness as a Key Factor Contributing to the Activation of Osmosensors and Essential Ras Signaling Pathways.Frontiers in cell and developmental biology · 2018Review
- Functional characterization of the upstream components of the Hog1-like kinase cascade in hyperosmotic and carbon sensing inBiotechnology for biofuels · 2018Article
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
In Saccharomyces cerevisiae, external high osmolarity activates the Hog1 mitogen-activated protein kinase (MAPK), which controls various aspects of osmoadaptation. Ssk1 is a homolog of bacterial two-component response regulators and activates the Ssk2 MAPK kinase kinase upstream of Hog1. It has been proposed that unphosphorylated Ssk1 (Ssk1-OH) is the active form and that Ssk1 phosphorylated (Ssk1 approximately P) at Asp554 by the Sln1-Ypd1-Ssk1 multistep phosphorelay mechanism is the inactive form. In this study, we show that constitutive activation of Ssk2 occurs when Ssk1 phosphorylation is blocked by either an Ssk1 mutation at the phosphorylation site or an Ssk1 mutation that inhibits its interaction with Ypd1, the donor of phosphate to Ssk1. Thus, Ssk1-OH is indeed necessary for Ssk2 activation. However, overexpression of wild-type Ssk1 or of an Ssk1 mutant that cannot bind Ssk2 prevents constitutively active Ssk1 mutants from activating Ssk2. Therefore, Ssk1 has a dual function as both an activator of Ssk2 and an inhibitor of Ssk1 itself. We also found that Ssk1 exists mostly as a dimer within cells. From mutant phenotypes, we deduce that only the Ssk1-OH/Ssk1-OH dimer can activate Ssk2 efficiently. Hence, because Ssk1 approximately P binds to and inhibits Ssk1-OH, moderate fluctuation of the level of Ssk1-OH does not lead to nonphysiological and detrimental activation of Hog1.
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