Evidence map›Paper›PMID 21813737›Full record

ArticleMolecular biology of the cell2011

Heat shock factor 2 is required for maintaining proteostasis against febrile-range thermal stress and polyglutamine aggregation.

Toyohide Shinkawa, Ke Tan, Mitsuaki Fujimoto, Naoki Hayashida, Kaoru Yamamoto, Eiichi Takaki, Ryosuke Takii, Ramachandran Prakasam, Sachiye Inouye, Valerie Mezger and 1 more

Abstract read
In one paragraph

Article in Molecular biology of the cell, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 35 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
35citing papers in PubMed, 1 pooled it
2.3field-weighted citation impact, top 12% 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

35 citing papers in PubMed, 1 synthesis or guideline pooled it, 75 citations in OpenAlex.

  1. Pooled it
  2. 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
  3. Review
  4. Review
  5. HSF1 Activation Mechanisms, Disease Roles, and Small Molecule Therapeutics.International journal of biological sciences · 2025
    Review
  6. Review
  7. Article
  8. HSF1 and Its Role in Huntington's Disease Pathology.Advances in experimental medicine and biology · 2023
    Review
  9. The function and regulation of heat shock transcription factor inFrontiers in cellular and infection microbiology · 2023
    Review
  10. Review
  11. Article
  12. Article
  13. The heat shock response and small molecule regulators.European journal of medicinal chemistry · 2021
    Review
  14. Article
  15. Article
  16. Article
  17. Article
  18. Review
  19. Tailoring of Proteostasis Networks with Heat Shock Factors.Cold Spring Harbor perspectives in biology · 2019
    Review
  20. 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

11 authors at 2 institutions in 2 countries.

Toyohide ShinkawaDepartment of Biochemistry and Molecular Biology, Yamaguchi University School of Medicine, Ube 755-8505, Japan.
Ke Tan
Mitsuaki Fujimoto
Naoki Hayashida
Kaoru Yamamoto
Eiichi Takaki
Ryosuke Takii
Ramachandran Prakasam
Sachiye Inouye
Valerie Mezger
Akira Nakai
Yamaguchi University · JPDélégation Paris 7 · FR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Heat shock response is characterized by the induction of heat shock proteins (HSPs), which facilitate protein folding, and non-HSP proteins with diverse functions, including protein degradation, and is regulated by heat shock factors (HSFs). HSF1 is a master regulator of HSP expression during heat shock in mammals, as is HSF3 in avians. HSF2 plays roles in development of the brain and reproductive organs. However, the fundamental roles of HSF2 in vertebrate cells have not been identified. Here we find that vertebrate HSF2 is activated during heat shock in the physiological range. HSF2 deficiency reduces threshold for chicken HSF3 or mouse HSF1 activation, resulting in increased HSP expression during mild heat shock. HSF2-null cells are more sensitive to sustained mild heat shock than wild-type cells, associated with the accumulation of ubiquitylated misfolded proteins. Furthermore, loss of HSF2 function increases the accumulation of aggregated polyglutamine protein and shortens the lifespan of R6/2 Huntington's disease mice, partly through αB-crystallin expression. These results identify HSF2 as a major regulator of proteostasis capacity against febrile-range thermal stress and suggest that HSF2 could be a promising therapeutic target for protein-misfolding diseases.

Indexed as

alpha-Crystallin B ChainAnimalsBrainChickensGene Expression RegulationHeat-Shock ProteinsHeat-Shock ResponseHumansHuntingtin ProteinMiceMice, Inbred C57BLMice, Inbred CBANerve Tissue ProteinsNuclear ProteinsPeptidesProtein Foldingalpha-Crystallin B ChainHeat-Shock ProteinsHsf2 protein, mouseHTT protein, humanHuntingtin ProteinNerve Tissue ProteinsNuclear ProteinsPeptidespolyglutamineTranscription Factors

Identifiers

PMID21813737
PMCPMC3183013
OpenAlexW2104693303

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-SA
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.