Evidence map›Paper›PMID 34616026›Full record

ArticleNature cell biology2021

Reversible amyloids of pyruvate kinase couple cell metabolism and stress granule disassembly.

Gea Cereghetti, Caroline Wilson-Zbinden, Vera M Kissling, Maren Diether, Alexandra Arm, Haneul Yoo, Ilaria Piazza, Shady Saad, Paola Picotti, D Allan Drummond and 3 more

Erratum issuedOpen access · greenAbstract read
In one paragraph

Article in Nature cell biology, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. 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
4.6field-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

35 citing papers in PubMed, 1 synthesis or guideline pooled it, 58 citations in OpenAlex.

  1. Pooled it
  2. Article
  3. Functional dissection ofProceedings of the National Academy of Sciences of the United States of America · 2026
    Article
  4. Small heat shock proteins and biomolecular condensates.Cellular and molecular life sciences : CMLS · 2026
    Review
  5. Article
  6. Article
  7. Histone Demethylase UTX Suppresses Tumor Cell Proliferation by Regulating Stress Granules.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2025
    Article
  8. Article
  9. Review
  10. Article
  11. Review
  12. Article
  13. Article
  14. Article
  15. Review
  16. The Heat Shock Response as a Condensate Cascade.Journal of molecular biology · 2024
    Review
  17. Review
  18. Article
  19. Article
  20. Mechanisms and pathology of protein misfolding and aggregation.Nature reviews. Molecular cell biology · 2023
    Review
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

13 authors at 3 institutions in 3 countries.

Gea CereghettiInstitute of Biochemistry, Department of Biology, ETH Zurich, Zurich, Switzerland.ORCID http://orcid.org/0000-0001-7732-9435
Caroline Wilson-Zbinden *Institute of Biochemistry, Department of Biology, ETH Zurich, Zurich, Switzerland.
Vera M Kissling *Institute of Biochemistry, Department of Biology, ETH Zurich, Zurich, Switzerland.ORCID http://orcid.org/0000-0002-4524-9905
Maren DietherInstitute of Molecular Systems Biology, ETH Zurich, Zurich, Switzerland.
Alexandra ArmInstitute of Biochemistry, Department of Biology, ETH Zurich, Zurich, Switzerland.
Haneul YooDepartment of Biochemistry and Molecular Biology, University of Chicago, Chicago, IL, USA.
Ilaria PiazzaInstitute of Molecular Systems Biology, ETH Zurich, Zurich, Switzerland.
Shady SaadInstitute of Biochemistry, Department of Biology, ETH Zurich, Zurich, Switzerland.ORCID http://orcid.org/0000-0003-1062-2906
Paola PicottiInstitute of Molecular Systems Biology, ETH Zurich, Zurich, Switzerland.
D Allan DrummondDepartment of Biochemistry and Molecular Biology, University of Chicago, Chicago, IL, USA.ORCID http://orcid.org/0000-0001-7018-7059
Uwe SauerInstitute of Molecular Systems Biology, ETH Zurich, Zurich, Switzerland.
Reinhard DechantInstitute of Biochemistry, Department of Biology, ETH Zurich, Zurich, Switzerland.ORCID http://orcid.org/0000-0002-4094-4773
Matthias PeterInstitute of Biochemistry, Department of Biology, ETH Zurich, Zurich, Switzerland. matthias.peter@bc.biol.ethz.ch.ORCID http://orcid.org/0000-0002-2160-6824
ETH Zurich · CHUniversity of Chicago · USMax Delbrück Center · DE

Funding

Signatures of interaction-driven selection on low-complexity sequencesR01GM127406 · NIGMS · UNIVERSITY OF CHICAGO · PI DRUMMOND, DAVID ALLAN · 2018 to 2021
$1.1M
NIGMS NIH HHS R01 GM127406Swiss National Science Foundation 200426
6 · The paper itself

Abstract

Cells respond to stress by blocking translation, rewiring metabolism and forming transient messenger ribonucleoprotein assemblies called stress granules (SGs). After stress release, re-establishing homeostasis and disassembling SGs requires ATP-consuming processes. However, the molecular mechanisms whereby cells restore ATP production and disassemble SGs after stress remain poorly understood. Here we show that upon stress, the ATP-producing enzyme Cdc19 forms inactive amyloids, and that their rapid re-solubilization is essential to restore ATP production and disassemble SGs in glucose-containing media. Cdc19 re-solubilization is initiated by the glycolytic metabolite fructose-1,6-bisphosphate, which directly binds Cdc19 amyloids, allowing Hsp104 and Ssa2 chaperone recruitment and aggregate re-solubilization. Fructose-1,6-bisphosphate then promotes Cdc19 tetramerization, which boosts its activity to further enhance ATP production and SG disassembly. Together, these results describe a molecular mechanism that is critical for stress recovery and directly couples cellular metabolism with SG dynamics via the regulation of reversible Cdc19 amyloids.

Indexed as

Stress, PhysiologicalAdenosine TriphosphateAmyloidCell Cycle ProteinsCytoplasmic GranulesFructosediphosphatesHeat-Shock ProteinsHSP70 Heat-Shock ProteinsPyruvate KinaseSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsAdenosine TriphosphateAmyloidCdc19 protein, S cerevisiaeCell Cycle Proteinsfructose-1,6-diphosphateFructosediphosphatesHeat-Shock ProteinsHsP104 protein, S cerevisiaeHSP70 Heat-Shock ProteinsPyruvate KinaseSaccharomyces cerevisiae ProteinsSSA2 protein, S cerevisiae

Identifiers

PMID34616026
PMCPMC7611853
OpenAlexW3138914839

What OpenQuestion holds

Textmetadata
LicenceTDM
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.