Evidence map›Paper›PMID 25135956›Full record

ArticleGenome research2014

H3S28 phosphorylation is a hallmark of the transcriptional response to cellular stress.

Anna Sawicka, Dominik Hartl, Malgorzata Goiser, Oliver Pusch, Roman R Stocsits, Ido M Tamir, Karl Mechtler, Christian Seiser

Open access · hybridAbstract read
In one paragraph

Article in Genome research, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 41 papers.

0numbers the graph read from it
0cells of the map it votes in
41citing papers in PubMed
–field-weighted citation impact
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

41 citing papers in PubMed, 62 citations in OpenAlex.

  1. Review
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  9. Investigation of the acetic acid stress response inMicrobial cell (Graz, Austria) · 2023
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  18. CaM kinase II regulates cardiac hemoglobin expression through histone phosphorylation upon sympathetic activation.Proceedings of the National Academy of Sciences of the United States of America · 2019
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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

8 authors at 5 institutions in 1 country.

Anna SawickaDepartment of Medical Biochemistry, Max F. Perutz Laboratories, Medical University of Vienna, Vienna Biocenter, 1030 Vienna, Austria;
Dominik HartlDepartment of Medical Biochemistry, Max F. Perutz Laboratories, Medical University of Vienna, Vienna Biocenter, 1030 Vienna, Austria;
Malgorzata GoiserDepartment of Medical Biochemistry, Max F. Perutz Laboratories, Medical University of Vienna, Vienna Biocenter, 1030 Vienna, Austria; Research Institute of Molecular Pathology, 1030 Vienna, Austria;
Oliver PuschCenter for Anatomy and Cell Biology, Medical University of Vienna, 1090 Vienna, Austria;
Roman R StocsitsResearch Institute of Molecular Pathology, 1030 Vienna, Austria;
Ido M TamirCampus Science Support Facilities GmbH, 1030 Vienna, Austria;
Karl MechtlerResearch Institute of Molecular Pathology, 1030 Vienna, Austria; Protein Chemistry Facility, IMBA Institute of Molecular Biotechnology of the Austrian Academy of Sciences, 1030 Vienna, Austria.
Christian SeiserDepartment of Medical Biochemistry, Max F. Perutz Laboratories, Medical University of Vienna, Vienna Biocenter, 1030 Vienna, Austria; christian.seiser@univie.ac.at.
Max Perutz Labs · ATResearch Institute of Molecular Pathology · ATCampus Science Support Facilities · ATInstitute of Molecular Biotechnology · ATMedical University of Vienna · AT

Funding

Austrian Science Fund FWF P 25807
6 · The paper itself

Abstract

The selectivity of transcriptional responses to extracellular cues is reflected by the deposition of stimulus-specific chromatin marks. Although histone H3 phosphorylation is a target of numerous signaling pathways, its role in transcriptional regulation remains poorly understood. Here, for the first time, we report a genome-wide analysis of H3S28 phosphorylation in a mammalian system in the context of stress signaling. We found that this mark targets as many as 50% of all stress-induced genes, underlining its importance in signal-induced transcription. By combining ChIP-seq, RNA-seq, and mass spectrometry we identified the factors involved in the biological interpretation of this histone modification. We found that MSK1/2-mediated phosphorylation of H3S28 at stress-responsive promoters contributes to the dissociation of HDAC corepressor complexes and thereby to enhanced local histone acetylation and subsequent transcriptional activation of stress-induced genes. Our data reveal a novel function of the H3S28ph mark in the activation of mammalian genes in response to MAP kinase pathway activation.

Indexed as

Transcriptional Activation3T3 CellsAcetylationAnimalsChromatin ImmunoprecipitationFibroblastsGene Expression ProfilingGene OntologyGenome-Wide Association StudyHeLa CellsHigh-Throughput Nucleotide SequencingHistone DeacetylasesHistonesHumansMAP Kinase Signaling SystemMiceHistone DeacetylasesHistonesmitogen and stress-activated protein kinase 1Ribosomal Protein S6 Kinases, 90-kDaSerine

Identifiers

PMID25135956
PMCPMC4216922
OpenAlexW2120903012

What OpenQuestion holds

Textmetadata
LicenceCC BY
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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.