Evidence map›Paper›PMID 36270993›Full record

ArticleNature communications2022

Translational reprogramming in response to accumulating stressors ensures critical threshold levels of Hsp90 for mammalian life.

Kaushik Bhattacharya, Samarpan Maiti, Szabolcs Zahoran, Lorenz Weidenauer, Dina Hany, Diana Wider, Lilia Bernasconi, Manfredo Quadroni, Martine Collart, Didier Picard

Open access · goldAbstract read
In one paragraph

Article in Nature communications, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.

0numbers the graph read from it
0cells of the map it votes in
24citing papers in PubMed
3.3field-weighted citation impact, top 6% 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

24 citing papers in PubMed, 40 citations in OpenAlex.

  1. Article
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  9. Review
  10. [EJNMMI radiopharmacy and chemistry · 2025
    Article
  11. Review
  12. Review
  13. In Vivo Visualization and Quantification of Brain Heat Shock Protein 90 with [Journal of nuclear medicine : official publication, Society of Nuclear Medicine · 2025
    Article
  14. Article
  15. Article
  16. Hsp90: Bringing it all together.Cell stress & chaperones · 2025
    Review
  17. Article
  18. Article
  19. Article
  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

10 authors at 2 institutions in 1 country.

Kaushik BhattacharyaDepartment of Molecular and Cellular Biology, University of Geneva, Geneva, Switzerland.
Samarpan MaitiDepartment of Molecular and Cellular Biology, University of Geneva, Geneva, Switzerland.
Szabolcs ZahoranDepartment of Microbiology and Molecular Medicine, University of Geneva, Geneva, Switzerland.
Lorenz WeidenauerProtein Analysis Facility, Center for Integrative Genomics, University of Lausanne, Lausanne, Switzerland.
Dina HanyDepartment of Molecular and Cellular Biology, University of Geneva, Geneva, Switzerland.ORCID 0000-0003-1872-8641
Diana WiderDepartment of Molecular and Cellular Biology, University of Geneva, Geneva, Switzerland.ORCID 0000-0002-7573-395X
Lilia BernasconiDepartment of Molecular and Cellular Biology, University of Geneva, Geneva, Switzerland.
Manfredo QuadroniProtein Analysis Facility, Center for Integrative Genomics, University of Lausanne, Lausanne, Switzerland.ORCID 0000-0002-2720-4084
Martine CollartDepartment of Microbiology and Molecular Medicine, University of Geneva, Geneva, Switzerland.ORCID 0000-0001-6955-1773
Didier PicardDepartment of Molecular and Cellular Biology, University of Geneva, Geneva, Switzerland. didier.picard@unige.ch.ORCID 0000-0001-8816-9668
University of Geneva · CHUniversity of Lausanne · CH

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The cytosolic molecular chaperone Hsp90 is essential for eukaryotic life. Although reduced Hsp90 levels correlate with aging, it was unknown whether eukaryotic cells and organisms can tune the basal Hsp90 levels to alleviate physiologically accumulated stress. We have investigated whether and how mice adapt to the deletion of three out of four alleles of the two genes encoding cytosolic Hsp90, with one Hsp90β allele being the only remaining one. While the vast majority of such mouse embryos die during gestation, survivors apparently manage to increase their Hsp90β protein to at least wild-type levels. Our studies reveal an internal ribosome entry site in the 5' untranslated region of the Hsp90β mRNA allowing translational reprogramming to compensate for the genetic loss of Hsp90 alleles and in response to stress. We find that the minimum amount of total Hsp90 required to support viability of mammalian cells and organisms is 50-70% of what is normally there. Those that fail to maintain a threshold level are subject to accelerated senescence, proteostatic collapse, and ultimately death. Therefore, considering that Hsp90 levels can be reduced ≥100-fold in the unicellular budding yeast, critical threshold levels of Hsp90 have markedly increased during eukaryotic evolution.

Indexed as

HSP90 Heat-Shock ProteinsInternal Ribosome Entry Sites5' Untranslated RegionsAnimalsMammalsMiceMolecular ChaperonesRNA, Messenger5' Untranslated RegionsHSP90 Heat-Shock ProteinsInternal Ribosome Entry SitesMolecular ChaperonesRNA, Messenger

Identifiers

PMID36270993
PMCPMC9587034
OpenAlexW4307139539

What OpenQuestion holds

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LicenceCC BY
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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.