Evidence map›Paper›PMID 20498630›Full record

ArticleOncogene2010

Roles of heat shock factor 1 and 2 in response to proteasome inhibition: consequence on p53 stability.

S Lecomte, F Desmots, F Le Masson, P Le Goff, D Michel, E S Christians, Y Le Dréan

Open access · bronzeAbstract read
PubMed Publisher
In one paragraph

Article in Oncogene, 2010. 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
1.5field-weighted citation impact, top 19% 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, 40 citations in OpenAlex.

  1. Review
  2. HSF1 and Its Role in Huntington's Disease Pathology.Advances in experimental medicine and biology · 2023
    Review
  3. Article
  4. Article
  5. Article
  6. Review
  7. Article
  8. Review
  9. Tailoring of Proteostasis Networks with Heat Shock Factors.Cold Spring Harbor perspectives in biology · 2019
    Review
  10. Roles of heat shock factor 1 beyond the heat shock response.Cellular and molecular life sciences : CMLS · 2018
    Review
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Review
  17. Article
  18. Article
  19. Article
  20. Article
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

7 authors at 3 institutions in 1 country.

S LecomteHoméostasie Intracellulaire des Protéines, UMR CNRS 6026, Interactions Cellulaires et Moléculaires, IFR 140-Génomique Fonctionnelle Agronomie et Santé-, Université de Rennes1, Rennes, France.
F Desmots
F Le Masson
P Le Goff
D Michel
E S Christians
Y Le Dréan
Centre National de la Recherche Scientifique · FRUniversité de Rennes · FRCentre de Biologie du Développement · FR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

A single heat shock factor (HSF), mediating the heat shock response, exists from yeast to Drosophila, whereas several related HSFs have been found in mammals. This raises the question of the specific or redundant functions of the different members of the HSF family and in particular of HSF1 and HSF2, which are both ubiquitously expressed. Using immortalized mouse embryonic fibroblasts (iMEFs) derived from wild-type, Hsf1(-/-), Hsf2(-/-) or double-mutant mice, we observed the distinctive behaviors of these mutants with respect to proteasome inhibition. This proteotoxic stress reduces to the same extent the viability of Hsf1(-/-)- and Hsf2(-/-)-deficient cells, but through different underlying mechanisms. Contrary to Hsf2(-/-) cells, Hsf1(-/-) cells are unable to induce pro-survival heat shock protein expression. Conversely, proteasome activity is lower in Hsf2(-/-) cells and the expression of some proteasome subunits, such as Psmb5 and gankyrin, is decreased. As gankyrin is an oncoprotein involved in p53 degradation, we analyzed the status of p53 in HSF-deficient iMEFs and observed that it was strongly stabilized in Hsf2(-/-) cells. This study points a new role for HSF2 in the regulation of protein degradation and suggests that pan-HSF inhibitors could be valuable tools to reduce chemoresistance to proteasome inhibition observed in cancer therapy.

Indexed as

Proteasome InhibitorsAnimalsCells, CulturedDNA-Binding ProteinsHeat-Shock ProteinsHeat Shock Transcription FactorsHSP70 Heat-Shock ProteinsMiceMolecular ChaperonesNeoplasm ProteinsNeoplasmsTranscription FactorsTumor Suppressor Protein p53UbiquitinDNA-Binding ProteinsHeat-Shock ProteinsHeat Shock Transcription FactorsHsbp1 protein, mouseHsf1 protein, mouseHsf2 protein, mouseHSP70 Heat-Shock ProteinsMolecular ChaperonesNeoplasm ProteinsProteasome InhibitorsTranscription FactorsTumor Suppressor Protein p53Ubiquitin

Identifiers

PMID20498630
OpenAlexW2094730469

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.