Evidence map›Paper›PMID 26152697›Full record

ArticleScience signaling2015

Proteotoxic stress reprograms the chromatin landscape of SUMO modification.

Anne Seifert, Pietà Schofield, Geoffrey J Barton, Ronald T Hay

Open access · greenAbstract read
In one paragraph

Article in Science signaling, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 48 papers.

0numbers the graph read from it
0cells of the map it votes in
48citing papers in PubMed
4.1field-weighted citation impact, top 5% 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

48 citing papers in PubMed, 93 citations in OpenAlex.

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  12. iScience · 2022
    Article
  13. Transcriptional lockdown during acute proteotoxic stress.Trends in biochemical sciences · 2022
    Review
  14. 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

4 authors at 1 institution in 1 country.

Anne SeifertCentre for Gene Regulation and Expression, College of Life Sciences, University of Dundee, Dundee, Scotland DD1 5EH, UK.
Pietà SchofieldCentre for Gene Regulation and Expression, College of Life Sciences, University of Dundee, Dundee, Scotland DD1 5EH, UK.
Geoffrey J BartonCentre for Gene Regulation and Expression, College of Life Sciences, University of Dundee, Dundee, Scotland DD1 5EH, UK.
Ronald T HayCentre for Gene Regulation and Expression, College of Life Sciences, University of Dundee, Dundee, Scotland DD1 5EH, UK. r.t.hay@dundee.ac.uk.
University of Dundee · GB

Funding

Medical Research Council G0701194Wellcome Trust 097945Wellcome Trust 097945/Z/11/ZWellcome Trust 098391Wellcome Trust 098391/Z/12/ZWellcome Trust 100476Wellcome Trust 100476/Z/12/Z
6 · The paper itself

Abstract

The small ubiquitin-like modifier 2 (SUMO-2) is required for survival when cells are exposed to treatments that induce proteotoxic stress by causing the accumulation of misfolded proteins. Exposure of cells to heat shock or other forms of proteotoxic stress induces the conjugation of SUMO-2 to proteins in the nucleus. We investigated the chromatin landscape of SUMO-2 modifications in response to heat stress. Through chromatin immunoprecipitation assays coupled to high-throughput DNA sequencing and mRNA sequencing, we showed that in response to heat shock, SUMO-2 accumulated at nucleosome-depleted, active DNA regulatory elements, which represented binding sites for large protein complexes and were predominantly associated with active genes. However, SUMO did not act as a direct transcriptional repressor or activator of these genes during heat shock. Instead, integration of our results with published proteomics data on heat shock-induced SUMO-2 substrates supports a model in which the conjugation of SUMO-2 to proteins acts as an acute stress response that is required for the stability of protein complexes involved in gene expression and posttranscriptional modification of mRNA. We showed that the conjugation of SUMO-2 to chromatin-associated proteins is an integral component of the proteotoxic stress response, and propose that SUMO-2 fulfills its essential role in cell survival by contributing to the maintenance of protein complex homeostasis.

Indexed as

Hot TemperatureStress, PhysiologicalBinding SitesCell Line, TumorCell SurvivalChromatinChromatin ImmunoprecipitationGene Expression RegulationHeat-Shock ResponseHigh-Throughput Nucleotide SequencingHumansProtein BindingRegulatory Elements, TranscriptionalReverse Transcriptase Polymerase Chain ReactionRNA, MessengerSmall Ubiquitin-Related Modifier ProteinsChromatinRNA, MessengerSmall Ubiquitin-Related Modifier ProteinsSUMO2 protein, human

Identifiers

PMID26152697
PMCPMC6707813
OpenAlexW2102679305

What OpenQuestion holds

Textmetadata
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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.