Evidence map›Paper›PMID 19129477›Full record

ArticleMolecular biology of the cell2009

Heterotrimerization of heat-shock factors 1 and 2 provides a transcriptional switch in response to distinct stimuli.

Anton Sandqvist, Johanna K Björk, Malin Akerfelt, Zhanna Chitikova, Alexei Grichine, Claire Vourc'h, Caroline Jolly, Tiina A Salminen, Yvonne Nymalm, Lea Sistonen

Open access · greenAbstract read
In one paragraph

Article in Molecular biology of the cell, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 85 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
85citing papers in PubMed, 1 pooled it
5.0field-weighted citation impact, top 4% 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

85 citing papers in PubMed, 1 synthesis or guideline pooled it, 157 citations in OpenAlex.

  1. Pooled it
  2. More than the 'master regulator of cytosolic proteostasis': new roles for HSF1 in promoting tissue health.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2026
    Review
  3. Adaptation to heat stress by diversification of the vertebrate heat shock transcription factor family.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2026
    Review
  4. Review
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  7. Review
  8. Article
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  10. HSF1 Activation Mechanisms, Disease Roles, and Small Molecule Therapeutics.International journal of biological sciences · 2025
    Review
  11. Article
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  13. Article
  14. Article
  15. Article
  16. Review
  17. HSF1 and Its Role in Huntington's Disease Pathology.Advances in experimental medicine and biology · 2023
    Review
  18. Article
  19. Review
  20. Article

25 more citing papers are in PubMed but not listed here.

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

10 authors at 2 institutions in 2 countries.

Anton SandqvistTurku Centre for Biotechnology, University of Turku, Abo Akademi University, 20520 Turku, Finland.
Johanna K Björk
Malin Akerfelt
Zhanna Chitikova
Alexei Grichine
Claire Vourc'h
Caroline Jolly
Tiina A Salminen
Yvonne Nymalm
Lea Sistonen
Åbo Akademi University · FIInserm · FR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Organisms respond to circumstances threatening the cellular protein homeostasis by activation of heat-shock transcription factors (HSFs), which play important roles in stress resistance, development, and longevity. Of the four HSFs in vertebrates (HSF1-4), HSF1 is activated by stress, whereas HSF2 lacks intrinsic stress responsiveness. The mechanism by which HSF2 is recruited to stress-inducible promoters and how HSF2 is activated is not known. However, changes in the HSF2 expression occur, coinciding with the functions of HSF2 in development. Here, we demonstrate that HSF1 and HSF2 form heterotrimers when bound to satellite III DNA in nuclear stress bodies, subnuclear structures in which HSF1 induces transcription. By depleting HSF2, we show that HSF1-HSF2 heterotrimerization is a mechanism regulating transcription. Upon stress, HSF2 DNA binding is HSF1 dependent. Intriguingly, when the elevated expression of HSF2 during development is mimicked, HSF2 binds to DNA and becomes transcriptionally competent. HSF2 activation leads to activation of also HSF1, revealing a functional interdependency that is mediated through the conserved trimerization domains of these factors. We propose that heterotrimerization of HSF1 and HSF2 integrates transcriptional activation in response to distinct stress and developmental stimuli.

Indexed as

Transcriptional ActivationAnimalsCell LineDNA-Binding ProteinsDNA, SatelliteHeat-Shock ProteinsHeat-Shock ResponseHeat Shock Transcription FactorsHumansMaleMiceTestisTranscription FactorsTranscription, GeneticDNA-Binding ProteinsDNA, SatelliteHeat-Shock ProteinsHeat Shock Transcription FactorsHSF1 protein, humanHSF2 protein, humanTranscription Factors

Identifiers

PMID19129477
PMCPMC2649261
OpenAlexW2150510467

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.