Evidence map›Paper›PMID 21253609›Full record

ArticlePloS one2011

Deciphering human heat shock transcription factor 1 regulation via post-translational modification in yeast.

Liliana Batista-Nascimento, Daniel W Neef, Phillip C C Liu, Claudina Rodrigues-Pousada, Dennis J Thiele

Open access · goldAbstract read
In one paragraph

Article in PloS one, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.

0numbers the graph read from it
0cells of the map it votes in
22citing papers in PubMed
2.0field-weighted citation impact, top 14% 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

22 citing papers in PubMed, 34 citations in OpenAlex.

  1. Article
  2. Article
  3. The Thermal Stress Coping Network of the NematodeInternational journal of molecular sciences · 2022
    Review
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  18. Article
  19. Review
  20. Heat shock response and insulin-associated neurodegeneration.Trends in pharmacological sciences · 2012
    Review
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 3 institutions in 2 countries.

Liliana Batista-NascimentoGenomics and Stress Laboratory, Instituto de Tecnologia Química e Biológica, Oeiras, Portugal.
Daniel W Neef
Phillip C C Liu
Claudina Rodrigues-Pousada
Dennis J Thiele
Duke University · USInstituto de Biologia Experimental e Tecnológica · PTIncyte (United States) · US

Funding

HSF1 as a therapeutic target in neurodegenerative diseaseR01NS065890 · NINDS · DUKE UNIVERSITY · PI THIELE, DENNIS J · 2010 to 2013
$1.3M
Stress regulation of RNA metabolismF32GM076954 · NIGMS · DUKE UNIVERSITY · PI NEEF, DANIEL W · 2006 to 2008
$99k
NIGMS NIH HHS F32 GM076954NIGMS NIH HHS GM076954NINDS NIH HHS R01 NS065890NINDS NIH HHS R01-NS065890
6 · The paper itself

Abstract

Heat shock transcription factor 1 (HSF1) plays an important role in the cellular response to proteotoxic stresses. Under normal growth conditions HSF1 is repressed as an inactive monomer in part through post-translation modifications that include protein acetylation, sumoylation and phosphorylation. Upon exposure to stress HSF1 homotrimerizes, accumulates in nucleus, binds DNA, becomes hyper-phosphorylated and activates the expression of stress response genes. While HSF1 and the mechanisms that regulate its activity have been studied for over two decades, our understanding of HSF1 regulation remains incomplete. As previous studies have shown that HSF1 and the heat shock response promoter element (HSE) are generally structurally conserved from yeast to metazoans, we have made use of the genetically tractable budding yeast as a facile assay system to further understand the mechanisms that regulate human HSF1 through phosphorylation of serine 303. We show that when human HSF1 is expressed in yeast its phosphorylation at S303 is promoted by the MAP-kinase Slt2 independent of a priming event at S307 previously believed to be a prerequisite. Furthermore, we show that phosphorylation at S303 in yeast and mammalian cells occurs independent of GSK3, the kinase primarily thought to be responsible for S303 phosphorylation. Lastly, while previous studies have suggested that S303 phosphorylation represses HSF1-dependent transactivation, we now show that S303 phosphorylation also represses HSF1 multimerization in both yeast and mammalian cells. Taken together, these studies suggest that yeast cells will be a powerful experimental tool for deciphering aspects of human HSF1 regulation by post-translational modifications.

Indexed as

Protein Processing, Post-TranslationalCloning, MolecularDNA-Binding ProteinsGlycogen Synthase Kinase 3Heat-Shock ResponseHeat Shock Transcription FactorsHumansPhosphorylationTranscription FactorsYeastsDNA-Binding ProteinsGlycogen Synthase Kinase 3Heat Shock Transcription FactorsHSF1 protein, humanTranscription Factors

Identifiers

PMID21253609
PMCPMC3017095
OpenAlexW2101837112

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Registered trials

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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.