Evidence map›Paper›PMID 32490574›Full record

ArticleThe EMBO journal2020

Feedback regulation of heat shock factor 1 (Hsf1) activity by Hsp70-mediated trimer unzipping and dissociation from DNA.

Szymon W Kmiecik, Laura Le Breton, Matthias P Mayer

Open access · hybridAbstract read
In one paragraph

Article in The EMBO journal, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 71 papers.

0numbers the graph read from it
0cells of the map it votes in
71citing papers in PubMed
4.3field-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

71 citing papers in PubMed, 110 citations in OpenAlex.

  1. Article
  2. Nutrients · 2026
    Article
  3. Review
  4. Article
  5. Principles and mechanisms of plant acclimation to heat stress.Nature reviews. Molecular cell biology · 2026
    Review
  6. Article
  7. An Amphibious Bifunctional Probe for Protein Chemical Cross-Linking.Journal of the American Chemical Society · 2026
    Article
  8. Article
  9. Article
  10. Article
  11. Review
  12. Article
  13. Mechanisms and regulation of the Hsp70 chaperone network.Nature reviews. Molecular cell biology · 2026
    Review
  14. Article
  15. Deciphering the role ofMicrobiology spectrum · 2026
    Article
  16. Review
  17. Review
  18. Sarcolipin but not phospholamban responds toFrontiers in physiology · 2026
    Article
  19. Article
  20. Review

11 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

3 authors at 1 institution in 1 country.

Szymon W KmiecikCenter for Molecular Biology of Heidelberg University (ZMBH), DKFZ-ZMBH-Alliance, Heidelberg, Germany.ORCID 0000-0001-6139-1680
Laura Le BretonCenter for Molecular Biology of Heidelberg University (ZMBH), DKFZ-ZMBH-Alliance, Heidelberg, Germany.
Matthias P MayerCenter for Molecular Biology of Heidelberg University (ZMBH), DKFZ-ZMBH-Alliance, Heidelberg, Germany.ORCID 0000-0002-7859-3112
Heidelberg University · DE

Funding

Deutsche Forschungsgemeinschaft SFB 1036 TP09
6 · The paper itself

Abstract

The heat shock response is a universal transcriptional response to proteotoxic stress orchestrated by heat shock transcription factor Hsf1 in all eukaryotic cells. Despite over 40 years of intense research, the mechanism of Hsf1 activity regulation remains poorly understood at the molecular level. In metazoa, Hsf1 trimerizes upon heat shock through a leucine-zipper domain and binds to DNA. How Hsf1 is dislodged from DNA and monomerized remained enigmatic. Here, using purified proteins, we demonstrate that unmodified trimeric Hsf1 is dissociated from DNA in vitro by Hsc70 and DnaJB1. Hsc70 binds to multiple sites in Hsf1 with different affinities. Hsf1 trimers are monomerized by successive cycles of entropic pulling, unzipping the triple leucine-zipper. Starting this unzipping at several protomers of the Hsf1 trimer results in faster monomerization. This process directly monitors the concentration of Hsc70 and DnaJB1. During heat shock adaptation, Hsc70 first binds to a high-affinity site in the transactivation domain, leading to partial attenuation of the response, and subsequently, at higher concentrations, Hsc70 removes Hsf1 from DNA to restore the resting state.

Indexed as

DNAHeat Shock Transcription FactorsHSC70 Heat-Shock ProteinsProtein MultimerizationAnimalsCell LineHSP40 Heat-Shock ProteinsHumansMiceMice, KnockoutProtein DomainsDNADNAJB1 protein, humanDnajb1 protein, mouseHeat Shock Transcription FactorsHSC70 Heat-Shock ProteinsHSF1 protein, humanHsf1 protein, mouseHSP40 Heat-Shock ProteinsHSPA8 protein, humanHspa8 protein, mouseattenuationDNA bindingentropic pullingheat shock responseHsp70

Identifiers

PMID32490574
PMCPMC7360973
OpenAlexW3032092131

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.