Evidence map›Paper›PMID 20430884›Full record

ArticleThe Journal of biological chemistry2010

The activity of yeast Hog1 MAPK is required during endoplasmic reticulum stress induced by tunicamycin exposure.

Francisco Torres-Quiroz, Sara García-Marqués, Roberto Coria, Francisca Randez-Gil, Jose A Prieto

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 33 papers.

0numbers the graph read from it
0cells of the map it votes in
33citing papers in PubMed
1.9field-weighted citation impact, top 16% 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

33 citing papers in PubMed, 63 citations in OpenAlex.

  1. HOG Signaling: A Multifunctional Regulator of Stress Homeostasis inJournal of fungi (Basel, Switzerland) · 2026
    Review
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  12. Adaptation to Endoplasmic Reticulum Stress inFrontiers in microbiology · 2021
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  16. Pho85 and PI(4,5)PBiochimica et biophysica acta. Molecular and cell biology of lipids · 2020
    Article
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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

5 authors at 2 institutions in 2 countries.

Francisco Torres-QuirozDepartment of Biotechnology, Instituto de Agroquímica y Tecnología de los Alimentos, Consejo Superior de Investigaciones Científicas, E-46100 Burjassot, Valencia, Spain.
Sara García-Marqués
Roberto Coria
Francisca Randez-Gil
Jose A Prieto
Consejo Superior de Investigaciones Científicas · ESUniversidad Nacional Autónoma de México · MX

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Accumulation of unfolded proteins in the endoplasmic reticulum (ER) triggers the so-called unfolded protein response (UPR), a conserved signaling pathway that drives the transcription of genes such as chaperones and folding enzymes. Nevertheless, the activity of the UPR accounts only for a part of the gene expression program activated upon ER stress. Moreover, the mechanism(s) for how cells adapt and survive to this stress are largely unknown. Here, we show that the yeast high osmolarity glycerol (HOG) pathway plays a role in ER stress resistance. Strains lacking the MAPK Hog1p displayed sensitivity to tunicamycin or beta-mercaptoethanol, whereas hyperactivation of the pathway enhanced their resistance. However, these effects were not due to Hog1p-mediated regulation of the UPR. Northern blot analysis demonstrated that Hog1p controls the tunicamycin-induced transcriptional change of GPD1 and that wild-type cells exposed to the drug accumulated glycerol in a Hog1p-dependent manner. Consistent with this, deletion of genes involved in glycerol synthesis caused increased sensitivity to tunicamycin, whereas overexpression of GPD1 provided higher tolerance to both wild-type and hog1Delta mutant cells. Quite remarkably, these effects were mediated by the basal activity of the MAPK because tunicamycin exposure does not trigger the phosphorylation of Hog1p or its nuclear import. Hence, our results describe new aspects of the yeast response to ER stress and identify additional functions of glycerol and the Hog1p MAPK to provide stress resistance.

Indexed as

Active Transport, Cell NucleusBlotting, WesternCell DivisionCell NucleusEndoplasmic ReticulumFungal ProteinsGlycerolHSP70 Heat-Shock ProteinsMicroscopy, FluorescenceMitogen-Activated Protein KinasesMutationPhosphorylationSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsSignal TransductionTranscription, GeneticFungal ProteinsGlycerolHOG1 protein, S cerevisiaeHSP70 Heat-Shock ProteinsKAR2 protein, yeastMitogen-Activated Protein KinasesSaccharomyces cerevisiae ProteinsTunicamycin

Identifiers

PMID20430884
PMCPMC2888421
OpenAlexW2024749532

What OpenQuestion holds

Textmetadata
Read underepoch 390

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.