Evidence map›Paper›PMID 32389298›Full record

ArticleFungal biology2020

Crosstalk between Saccharomycescerevisiae SAPKs Hog1 and Mpk1 is mediated by glycerol accumulation.

Ekaterina V Laz, Jongmin Lee, David E Levin

Open access · greenAbstract read
In one paragraph

Article in Fungal biology, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.

0numbers the graph read from it
0cells of the map it votes in
11citing papers in PubMed
0.6field-weighted citation impact, top 33% 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

11 citing papers in PubMed, 15 citations in OpenAlex.

  1. Article
  2. Development ofBiotechnology reports (Amsterdam, Netherlands) · 2026
    Article
  3. Review
  4. Review
  5. Article
  6. Article
  7. Article
  8. Control of Gene Expression via the Yeast CWI Pathway.International journal of molecular sciences · 2022
    Review
  9. Review
  10. Article
  11. 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

3 authors at 1 institution in 1 country.

Ekaterina V LazDepartment of Molecular and Cell Biology, Boston University Goldman School of Dental Medicine, Boston, MA, USA.
Jongmin LeeDepartment of Molecular and Cell Biology, Boston University Goldman School of Dental Medicine, Boston, MA, USA.
David E LevinDepartment of Molecular and Cell Biology, Boston University Goldman School of Dental Medicine, Boston, MA, USA; Department of Microbiology, Boston University School of Medicine, Boston, MA, USA. Electronic address: delevin@bu.edu.
Boston University · US

Funding

ROLE OF PROTEIN KINASE C IN YEAST GROWTH CONTROLR01GM048533 · NIGMS · JOHNS HOPKINS UNIVERSITY · PI LEVIN, DAVID E. · 1992 to 2025
$7.8M
The Arsenic Stress Signaling Code of YeastR01GM138413 · NIGMS · BOSTON UNIVERSITY MEDICAL CAMPUS · PI LEVIN, DAVID E. · 2020 to 2023
$1.8M
NIGMS NIH HHS R01 GM048533NIGMS NIH HHS R01 GM138413
6 · The paper itself

Abstract

Two stress-activated MAP kinase (SAPK) pathways in Saccharomyces cerevisiae respond to osmotic imbalances. The High Osmolarity Glycerol (HOG) pathway is activated in response to hyper-osmotic stress, whereas the Cell Wall Integrity (CWI) pathway is activated in response to hypo-osmotic stress. However, there is also evidence of complex interplay and crosstalk between the two pathways. For example, treatment with zymolyase, a mixture of cell wall degrading enzymes, is known to activate the SAPK Hog1 of the HOG pathway and the SAPK Mpk1 of the CWI pathway sequentially, with Mpk1 activation dependent upon Hog1. Additionally, the PTP2- and PTP3-encoded tyrosine-specific protein phosphatases play a key role in down-regulation of Hog1, but may also down-regulate Mpk1. In this study, we show that hyperactivation of Mpk1 in a ptp2 ptp3 null mutant is an indirect consequence of Hog1 hyperactivation, which induces accumulation of intracellular glycerol and an attendant hypo-osmotic stress. Mpk1 hyperactivity in the absence of PTP2 and PTP3 was suppressed by a hog1 null mutation, or by restoration of osmotic balance with a constitutive form of the glycerol channel Fps1. We found similarly that activation of Mpk1 in response to zymolyase treatment is partly a consequence of Hog1-driven glycerol accumulation. Thus, we have identified two conditions in which glycerol serves as a mediator of crosstalk between the HOG and CWI pathways.

Indexed as

GlycerolMitogen-Activated Protein KinasesSaccharomyces cerevisiae ProteinsEnzyme ActivationMutationOsmotic PressurePhosphorylationSaccharomyces cerevisiaeGlycerolHOG1 protein, S cerevisiaeMitogen-Activated Protein KinasesSaccharomyces cerevisiae ProteinsSLT2 protein, S cerevisiaeCWI pathwayHOG pathwayOsmotic imbalancePtp2Ptp3Zymolyase

Identifiers

PMID32389298
PMCPMC7217976
OpenAlexW2981171510

What OpenQuestion holds

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Registered trials

None linked

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.