Evidence map›Paper›PMID 32011004›Full record

ArticleThe EMBO journal2020

Osmostress enhances activating phosphorylation of Hog1 MAP kinase by mono-phosphorylated Pbs2 MAP2K.

Kazuo Tatebayashi, Katsuyoshi Yamamoto, Taichiro Tomida, Akiko Nishimura, Tomomi Takayama, Masaaki Oyama, Hiroko Kozuka-Hata, Satomi Adachi-Akahane, Yuji Tokunaga, Haruo Saito

Open access · hybridAbstract read
In one paragraph

Article in The EMBO journal, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 36 papers.

0numbers the graph read from it
0cells of the map it votes in
36citing papers in PubMed
3.0field-weighted citation impact, top 8% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

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.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

36 citing papers in PubMed, 57 citations in OpenAlex.

  1. HOG Signaling: A Multifunctional Regulator of Stress Homeostasis inJournal of fungi (Basel, Switzerland) · 2026
    Review
  2. Review
  3. Article
  4. Article
  5. Review
  6. Article
  7. EvaluatingFrontiers in microbiology · 2026
    Article
  8. Surprising regulatory plasticity for the conserved HOG pathway in diversebioRxiv : the preprint server for biology · 2025
    Article
  9. Review
  10. Article
  11. Article
  12. Pbs2 regulates late-stage macroautophagy in Saccharomyces cerevisiae.Animal models and experimental medicine · 2025
    Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Review
  19. Article
  20. Metabolome and Mycobiome ofPlants (Basel, Switzerland) · 2024
    Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

10 authors at 3 institutions in 1 country.

Kazuo TatebayashiLaboratory of Molecular Genetics, Frontier Research Unit, Institute of Medical Science, The University of Tokyo, Tokyo, Japan.ORCID 0000-0002-3131-7030
Katsuyoshi YamamotoDivision of Molecular Cell Signaling, Institute of Medical Science, The University of Tokyo, Tokyo, Japan.
Taichiro TomidaDepartment of Physiology, School of Medicine, Faculty of Medicine, Toho University, Tokyo, Japan.
Akiko NishimuraDivision of Molecular Cell Signaling, Institute of Medical Science, The University of Tokyo, Tokyo, Japan.
Tomomi TakayamaDivision of Molecular Cell Signaling, Institute of Medical Science, The University of Tokyo, Tokyo, Japan.
Masaaki OyamaMedical Proteomics Laboratory, Institute of Medical Science, The University of Tokyo, Tokyo, Japan.
Hiroko Kozuka-HataMedical Proteomics Laboratory, Institute of Medical Science, The University of Tokyo, Tokyo, Japan.
Satomi Adachi-AkahaneDepartment of Physiology, School of Medicine, Faculty of Medicine, Toho University, Tokyo, Japan.
Yuji TokunagaMolecular Profiling Research Center for Drug Discovery, National Institute of Advanced Industrial Science and Technology, Tokyo, Japan.
Haruo SaitoDivision of Molecular Cell Signaling, Institute of Medical Science, The University of Tokyo, Tokyo, Japan.ORCID 0000-0001-7891-1689
The University of Tokyo · JPToho University · JPNational Institute of Advanced Industrial Science and Technology · JP

Funding

GPLLI program from MEXTJapan Foundation for Applied EnzymologyMEXT | Japan Society for the Promotion of Science (JSPS) 16H04761MEXT | Japan Society for the Promotion of Science (JSPS) 16H06578MEXT | Japan Society for the Promotion of Science (JSPS) 17H06017MEXT | Japan Society for the Promotion of Science (JSPS) 17K15083MEXT | Japan Society for the Promotion of Science (JSPS) 19K06548MEXT | Japan Society for the Promotion of Science (JSPS) 24247034MEXT | Japan Society for the Promotion of Science (JSPS) 25440042Mochida Memorial Foundation for Medical and Pharmaceutical ResearchSalt Science Research Foundation 1732Sumitomo Foundation 150075
6 · The paper itself

Abstract

The MAP kinase (MAPK) Hog1 is the central regulator of osmoadaptation in yeast. When cells are exposed to high osmolarity, the functionally redundant Sho1 and Sln1 osmosensors, respectively, activate the Ste11-Pbs2-Hog1 MAPK cascade and the Ssk2/Ssk22-Pbs2-Hog1 MAPK cascade. In a canonical MAPK cascade, a MAPK kinase kinase (MAP3K) activates a MAPK kinase (MAP2K) by phosphorylating two conserved Ser/Thr residues in the activation loop. Here, we report that the MAP3K Ste11 phosphorylates only one activating phosphorylation site (Thr-518) in Pbs2, whereas the MAP3Ks Ssk2/Ssk22 can phosphorylate both Ser-514 and Thr-518 under optimal osmostress conditions. Mono-phosphorylated Pbs2 cannot phosphorylate Hog1 unless the reaction between Pbs2 and Hog1 is enhanced by osmostress. The lack of the osmotic enhancement of the Pbs2-Hog1 reaction suppresses Hog1 activation by basal MAP3K activities and prevents pheromone-to-Hog1 crosstalk in the absence of osmostress. We also report that the rapid-and-transient Hog1 activation kinetics at mildly high osmolarities and the slow and prolonged activation kinetics at severely high osmolarities are both caused by a common feedback mechanism.

Indexed as

HEK293 CellsHumansIntracellular Signaling Peptides and ProteinsMAP Kinase Kinase KinasesMAP Kinase Signaling SystemMembrane ProteinsMitogen-Activated Protein Kinase KinasesMitogen-Activated Protein KinasesOsmolar ConcentrationPheromonesPhosphorylationProtein KinasesSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsStress, PhysiologicalHOG1 protein, S cerevisiaeIntracellular Signaling Peptides and ProteinsMAP Kinase Kinase KinasesMembrane ProteinsMitogen-Activated Protein Kinase KinasesMitogen-Activated Protein KinasesPBS2 protein, S cerevisiaePheromonesProtein KinasesSaccharomyces cerevisiae ProteinsSHO1 protein, S cerevisiaeSLN1 protein, S cerevisiaeSte11 protein, S cerevisiaeHog1HOG pathwayMAP kinaseosmostresssignal transduction

Identifiers

PMID32011004
PMCPMC7049814
OpenAlexW3004323549

What OpenQuestion holds

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LicenceCC BY
Read underepoch 390

Registered trials

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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.