ArticleGenes & development2013
MAPK Hog1 closes the S. cerevisiae glycerol channel Fps1 by phosphorylating and displacing its positive regulators.
Article in Genes & development, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 64 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
64 citing papers in PubMed, 113 citations in OpenAlex.
- Hog1 plays a role in regulating lipid droplet homeostasis.Archives of microbiology · 2025Article
- Acetic acid-induced stress granules function as scaffolding complexes for Hog1 activation by Pbs2.The Journal of cell biology · 2025Article
- Glycerol bioconversion to biofuel and value-added products by yeasts.FEMS yeast research · 2025Review
- Article
- The relationship mammalian p38 with human health and its homolog Hog1 in response to environmental stresses inFrontiers in cell and developmental biology · 2025Review
- The Viral K1 Killer Yeast System: Toxicity, Immunity, and Resistance.Yeast (Chichester, England) · 2024Review
- Engineering of Aspergillus niger for efficient production of D-xylitol from L-arabinose.Microbial cell factories · 2024Article
- Multilevel Regulation of Membrane Proteins in Response to Metal and Metalloid Stress: A Lesson from Yeast.International journal of molecular sciences · 2024Review
- Aspergillus fumigatus mitogen-activated protein kinase MpkA is involved in gliotoxin production and self-protection.Nature communications · 2024Article
- General mechanisms of weak acid-tolerance and current strategies for the development of tolerant yeasts.World journal of microbiology & biotechnology · 2023Review
- Phenotypic consequences of logarithmic signaling in MAPK stress response.bioRxiv : the preprint server for biology · 2023Article
- IntracellularProceedings of the National Academy of Sciences of the United States of America · 2023Article
- Activation of CWI pathway through high hydrostatic pressure, enhancing glycerol efflux via the aquaglyceroporin Fps1 inMolecular biology of the cell · 2023Article
- The regulatory mechanism of the yeast osmoresponse under different glucose concentrations.iScience · 2023Article
- Adaptation of the yeast gene knockout collection is near-perfectly predicted by fitness and diminishing return epistasis.G3 (Bethesda, Md.) · 2022Article
- The role of the glycerol transporter channel Fps1p in cellular proteostasis during enhanced proteotoxic stress.Applied microbiology and biotechnology · 2022Article
- Yeast osmoregulation - glycerol still in pole position.FEMS yeast research · 2022Review
- CRISPR-Cas9 Approach Constructed EngineeredJournal of fungi (Basel, Switzerland) · 2022Article
- Insights into the glycerol transport of Yarrowia lipolytica.Yeast (Chichester, England) · 2022Article
- Differential metabolism of arsenicals regulates Fps1-mediated arsenite transport.The Journal of cell biology · 2022Article
4 more citing papers are in PubMed but not listed here.
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
8 authors at 4 institutions in 2 countries.
Funding
Abstract
The aquaglyceroprin Fps1 is responsible for glycerol transport in yeast in response to changes in extracellular osmolarity. Control of Fps1 channel activity in response to hyperosmotic shock involves a redundant pair of regulators, Rgc1 (regulator of the glycerol channel 1) and Rgc2, and the MAPK Hog1 (high-osmolarity glycerol response 1). However, the mechanism by which these factors influence channel activity is unknown. We show that Rgc2 maintains Fps1 in the open channel state in the absence of osmotic stress by binding to its C-terminal cytoplasmic domain. This interaction involves a tripartite pleckstrin homology (PH) domain within Rgc2 and a partial PH domain within Fps1. Activation of Hog1 in response to hyperosmotic shock induces the rapid eviction of Rgc2 from Fps1 and consequent channel closure. Hog1 was recruited to the N-terminal cytoplasmic domain of Fps1, which it uses as a platform from which to multiply phosphorylate Rgc2. Thus, these results reveal the mechanism by which Hog1 regulates Fps1 in response to hyperosmotic shock.
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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.