Evidence map›Paper›PMID 36574355›Full record

ArticleThe EMBO journal2023

Cytosolic stress granules relieve the ubiquitin-proteasome system in the nuclear compartment.

Shanshan Xu, Maria E Gierisch, Anna Katharina Schellhaus, Ina Poser, Simon Alberti, Florian A Salomons, Nico P Dantuma

Open access · hybridAbstract read
In one paragraph

Article in The EMBO journal, 2023. 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
1.7field-weighted citation impact, top 15% 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, 20 citations in OpenAlex.

  1. Review
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  4. Article
  5. Review
  6. Review
  7. Article
  8. Review
  9. Review
  10. Article
  11. Review
  12. Proteasome dynamics in response to metabolic changes.Frontiers in cell and developmental biology · 2025
    Review
  13. Article
  14. Article
  15. Article
  16. Article
  17. Molecular hallmarks of ageing in amyotrophic lateral sclerosis.Cellular and molecular life sciences : CMLS · 2024
    Review
  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 2 countries.

Shanshan XuDepartment of Cell and Molecular Biology (CMB), Karolinska Institutet, Stockholm, Sweden.ORCID 0000-0001-9875-3403
Maria E GierischDepartment of Cell and Molecular Biology (CMB), Karolinska Institutet, Stockholm, Sweden.ORCID 0000-0002-8053-4402
Anna Katharina SchellhausDepartment of Cell and Molecular Biology (CMB), Karolinska Institutet, Stockholm, Sweden.
Ina PoserMax Planck Institute of Molecular Cell Biology and Genetics, Dresden, Germany.ORCID 0000-0002-9108-1592
Simon AlbertiMax Planck Institute of Molecular Cell Biology and Genetics, Dresden, Germany.ORCID 0000-0003-4017-6505
Florian A SalomonsDepartment of Cell and Molecular Biology (CMB), Karolinska Institutet, Stockholm, Sweden.
Nico P DantumaDepartment of Cell and Molecular Biology (CMB), Karolinska Institutet, Stockholm, Sweden.ORCID 0000-0002-6090-4170
Karolinska Institutet · SECenter for Systems Biology Dresden · DEMax Planck Institute of Molecular Cell Biology and Genetics · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The role of cytosolic stress granules in the integrated stress response has remained largely enigmatic. Here, we studied the functionality of the ubiquitin-proteasome system (UPS) in cells that were unable to form stress granules. Surprisingly, the inability of cells to form cytosolic stress granules had primarily a negative impact on the functionality of the nuclear UPS. While defective ribosome products (DRiPs) accumulated at stress granules in thermally stressed control cells, they localized to nucleoli in stress granule-deficient cells. The nuclear localization of DRiPs was accompanied by redistribution and enhanced degradation of SUMOylated proteins. Depletion of the SUMO-targeted ubiquitin ligase RNF4, which targets SUMOylated misfolded proteins for proteasomal degradation, largely restored the functionality of the UPS in the nuclear compartment in stress granule-deficient cells. Stress granule-deficient cells showed an increase in the formation of mutant ataxin-1 nuclear inclusions when exposed to thermal stress. Our data reveal that stress granules play an important role in the sequestration of cytosolic misfolded proteins, thereby preventing these proteins from accumulating in the nucleus, where they would otherwise infringe nuclear proteostasis.

Indexed as

Proteasome Endopeptidase ComplexUbiquitinNuclear ProteinsStress GranulesTranscription FactorsNuclear ProteinsProteasome Endopeptidase ComplexTranscription FactorsUbiquitinprotein quality controlproteostasisstress granulesSUMOubiquitin-proteasome system

Identifiers

PMID36574355
PMCPMC9890234
OpenAlexW4313249967

What OpenQuestion holds

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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.