Evidence map›Paper›PMID 31772124›Full record

ArticleScience signaling2019

Thiol-based direct threat sensing by the stress-activated protein kinase Hog1.

Angel Guerra-Moreno, Miguel A Prado, Jessie Ang, Helena M Schnell, Yagmur Micoogullari, Joao A Paulo, Daniel Finley, Steven P Gygi, John Hanna

Open access · greenAbstract read
In one paragraph

Article in Science signaling, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.

0numbers the graph read from it
0cells of the map it votes in
10citing papers in PubMed
0.6field-weighted citation impact, top 32% 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

10 citing papers in PubMed, 15 citations in OpenAlex.

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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

9 authors at 2 institutions in 1 country.

Angel Guerra-MorenoDepartment of Pathology, Brigham and Women's Hospital and Harvard Medical School, Boston, MA, USA.ORCID 0000-0003-2321-1129
Miguel A PradoDepartment of Cell Biology, Harvard Medical School, Boston, MA, USA.ORCID 0000-0002-4914-1619
Jessie AngDepartment of Pathology, Brigham and Women's Hospital and Harvard Medical School, Boston, MA, USA.ORCID 0000-0002-9621-9415
Helena M SchnellDepartment of Pathology, Brigham and Women's Hospital and Harvard Medical School, Boston, MA, USA.ORCID 0000-0002-7840-4473
Yagmur MicoogullariDepartment of Pathology, Brigham and Women's Hospital and Harvard Medical School, Boston, MA, USA.
Joao A PauloDepartment of Cell Biology, Harvard Medical School, Boston, MA, USA.ORCID 0000-0002-4291-413X
Daniel FinleyDepartment of Cell Biology, Harvard Medical School, Boston, MA, USA.ORCID 0000-0003-2076-5863
Steven P GygiDepartment of Cell Biology, Harvard Medical School, Boston, MA, USA.ORCID 0000-0001-7626-0034
John HannaDepartment of Pathology, Brigham and Women's Hospital and Harvard Medical School, Boston, MA, USA. jwhanna@bwh.harvard.edu.ORCID 0000-0003-2964-1058
Brigham and Women's Hospital · USHarvard University · US

Funding

New Sample Multiplexing Technologies to Identify Chemical Probes and Illuminate Ubiquitin BiologyR01GM067945 · NIGMS · HARVARD UNIVERSITY (MEDICAL SCHOOL) · PI GYGI, STEVEN P · 2003 to 2024
$10.5M
UBIQUITIN-PROTEIN CONJUGATES AND FUSIONSR01GM043601 · NIGMS · HARVARD UNIVERSITY (MEDICAL SCHOOL) · PI FINLEY, DANIEL J · 1990 to 2020
$4.3M
New Ubiquitin-Proteasome System Components that Protect against ProteotoxicityDP5OD019800 · OD · BRIGHAM AND WOMEN'S HOSPITAL · PI HANNA, JOHN W · 2014 to 2018
$2.2M
Advancing Multiplexed Isobaric Tag-based Strategies for Proteome ProfilingR01GM132129 · NIGMS · HARVARD MEDICAL SCHOOL · PI PAULO, JOAO A · 2019 to 2023
$1.7M
Resolving the role of nicotine-mediated phosphorylation on pancreatic fibrosisK01DK098285 · NIDDK · HARVARD MEDICAL SCHOOL · PI PAULO, JOAO A · 2013 to 2017
$638k
NIDDK NIH HHS K01 DK098285NIGMS NIH HHS R01 GM043601NIGMS NIH HHS R01 GM067945NIGMS NIH HHS R01 GM132129NIH HHS DP5 OD019800
6 · The paper itself

Abstract

The yeast stress-activated protein kinase Hog1 is best known for its role in mediating the response to osmotic stress, but it is also activated by various mechanistically distinct environmental stressors, including heat shock, endoplasmic reticulum stress, and arsenic. In the osmotic stress response, the signal is sensed upstream and relayed to Hog1 through a kinase cascade. Here, we identified a mode of Hog1 function whereby Hog1 senses arsenic through a direct physical interaction that requires three conserved cysteine residues located adjacent to the catalytic loop. These residues were essential for Hog1-mediated protection against arsenic, were dispensable for the response to osmotic stress, and promoted the nuclear localization of Hog1 upon exposure of cells to arsenic. Hog1 promoted arsenic detoxification by stimulating phosphorylation of the transcription factor Yap8, promoting Yap8 nuclear localization, and stimulating the transcription of the only known Yap8 targets,

Indexed as

Arsenate ReductasesArsenicBasic-Leucine Zipper Transcription FactorsMAP Kinase Signaling SystemMitogen-Activated Protein KinasesSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsARR1 protein, S cerevisiaeARR2 protein, S cerevisiaeArsenate ReductasesArsenicBasic-Leucine Zipper Transcription FactorsHOG1 protein, S cerevisiaeMitogen-Activated Protein KinasesSaccharomyces cerevisiae Proteins

Identifiers

PMID31772124
PMCPMC7263400
OpenAlexW2991107158

What OpenQuestion holds

Textmetadata
LicenceTDM
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.