Delayed Turnover of Unphosphorylated Ssk1 during Carbon Stress Activates the Yeast Hog1 Map Kinase Pathway
Open accessAbstract
In Saccharomyces cerevisiae, the Hog1 mitogen-activated protein kinase (MAPK) pathway coordinates the adaptation to osmotic stress and was recently reported to respond to acute changes in glucose levels. Similarly as in osmotic stress, glucose starvation leads to a transient accumulation of Hog1 in the nucleus. However, the kinetics and the mechanism of Hog1 activation are different for these stress conditions. During osmotic shock the activation of Hog1 can be transduced by either the Sho1 or the Sln1/Ypd1/Ssk1 branch. During glucose starvation the phosphorylation of Hog1 is slower and is completely dependent on Ssk1, but independent of Sho1. To characterize the mechanism of activation of Hog1 during carbon stress, we examined the turnover of Ssk1 protein levels upon glucose starvation in the presence of cycloheximide and monitored protein levels by western blotting. Our data demonstrate that unphosphorylated Ssk1 was quickly degraded during exponential growth and after osmotic stress but remained remarkably stable during glucose limitation. We conclude that glucose starvation induces a delay in the turnover of unphosphorylated Ssk1, which is sufficient to activate the Hog1 MAPK pathway. Although unphosphorylated Ssk1 is known to be degraded by the proteasome, its stabilization is apparently not due to changes in cellular localization or decrease in ubiquitination levels during glucose limitation.
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Snf1 and Hog1 MAPK regulate global changes in gene expressions for utilizing alternate carbon sources in Crabtree-positive yeasts upon phosphorylation.
“Also, the Snf1 and the Hog1 MAPK regulate global changes in gene expressions for utilizing alternate carbon sources in Crabtree-positive yeasts upon phosphorylation (27, 28)”
From Divergent mitochondrial responses and metabolic signal pathways secure the azole resistance in Crabtree-positive and negative <i>Candida</i> species (2024) · cites this paper as [28]
The Results (page unavailable) say Snf1 regulates genes needed to use other carbon sources and show that glucose starvation induces Hog1 phosphorylation. The Introduction says Hog1 can regulate transcription factors, but the paper does not establish that Snf1 and Hog1 together regulate global gene-expression changes for alternative-carbon-source use in Crabtree-positive yeasts. (LLM, conf=0.86)
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- Authors
- Vallejo, M. C., & Mayinger, P.
- Affiliations
- Oregon Health & Science University (US)
- Corresponding author
- Mayinger, Peter
- ORCID
- Mayinger, Peter
- Venue
- PLOS ONE
- Publisher
- Public Library of Science (PLoS)
- Published
- 2015-09-04
- Volume
- 10
- Issue
- 9
- Pages
- e0137199
- ISSN
- 1932-6203 (ISSN-L)
- PMC
- PMC4560374
- OpenAlex
- W2112879334
- Cited by
- 14
- References
- 28
- Citations by year
- 2025: 1 · 2024: 2 · 2023: 3 · 2022: 1 · 2019: 1 · 2018: 2 · 2017: 3 · 2016: 1
- FWCI
- 0.87
- Type
- journal article
- Language
- en
- Open access
- gold
- doi.org
- Licence
- Locations
- PLoS ONE (publishedVersion, cc-by)
- Europe PMC (PubMed Central) (publishedVersion, cc-by)
- PubMed Central (publishedVersion, cc-by)
- PubMed (publishedVersion)
- DOAJ (DOAJ: Directory of Open Access Journals) (submittedVersion, cc-by-sa)
- Funders
- National Institutes of Health
- National Institute of General Medical Sciences (R01GM084088)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Fungal and yeast genetics research
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Genetics › Bacterial Genetics and Biotechnology
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Kinase Regulation and GTPase Signaling
- Keywords
- SSK1, glucose deprivation, carbon stress, protein turnover, osmotic stress, Sho1, protein stability, proteasomal degradation, Saccharomyces cerevisiae, stress adaptation
- MeSH terms
- Cycloheximide, Glucose, Leupeptins, Membrane Proteins, Osmotic Pressure, Phosphorylation, Protein Kinases, Protein Synthesis Inhibitors, Saccharomyces cerevisiae, Sodium Chloride, Stress, Physiological, Signal Transduction, Gene Expression Regulation, Fungal, Mitogen-Activated Protein Kinases, Saccharomyces cerevisiae Proteins, Proteasome Endopeptidase Complex, Intracellular Signaling Peptides and Proteins, Ubiquitination, Proteolysis
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