Evidence map›Paper›PMID 35148816›Full record

ArticleMolecular cell2022

Chaperones directly and efficiently disperse stress-triggered biomolecular condensates.

Haneul Yoo, Jared A M Bard, Evgeny V Pilipenko, D Allan Drummond

Open access · greenAbstract read
In one paragraph

Article in Molecular cell, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 79 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
79citing papers in PubMed, 1 pooled it
9.1field-weighted citation impact, top 1% 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

79 citing papers in PubMed, 1 synthesis or guideline pooled it, 108 citations in OpenAlex.

  1. Pooled it
  2. Review
  3. Article
  4. Article
  5. Article
  6. Small heat shock proteins and biomolecular condensates.Cellular and molecular life sciences : CMLS · 2026
    Review
  7. Review
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Accurate prediction of thermoresponsive phase behavior of disordered proteins.Protein science : a publication of the Protein Society · 2025
    Article
  18. Review
  19. Review
  20. Article

19 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

4 authors at 1 institution in 1 country.

Haneul YooDepartment of Biochemistry and Molecular Biology, The University of Chicago, Chicago, IL 60637, USA.
Jared A M BardDepartment of Biochemistry and Molecular Biology, The University of Chicago, Chicago, IL 60637, USA.
Evgeny V PilipenkoDepartment of Biochemistry and Molecular Biology, The University of Chicago, Chicago, IL 60637, USA.
D Allan DrummondDepartment of Biochemistry and Molecular Biology, The University of Chicago, Chicago, IL 60637, USA; Department of Medicine, Section of Genetic Medicine, The University of Chicago, Chicago, IL 60637, USA. Electronic address: dadrummond@uchicago.edu.
University of Chicago · US

Funding

Molecular And Cellular Biology Training ProgramT32GM007183 · NIGMS · UNIVERSITY OF CHICAGO · PI GLICK, BENJAMIN S, RICE, PHOEBE A · 1985 to 2021
$23.9M
Function and Regulation of Stress-Induced Adaptive CondensatesR35GM144278 · NIGMS · UNIVERSITY OF CHICAGO · PI David Allan Drummond · 2022 to 2026
$2.6M
Determining the molecular basis of adaptive stress-triggered protein phase separationR01GM126547 · NIGMS · UNIVERSITY OF CHICAGO · PI DRUMMOND, DAVID ALLAN, SOSNICK, TOBIN R · 2018 to 2021
$1.6M
Signatures of interaction-driven selection on low-complexity sequencesR01GM127406 · NIGMS · UNIVERSITY OF CHICAGO · PI DRUMMOND, DAVID ALLAN · 2018 to 2021
$1.1M
Investigating the disaggregation of stress-induced phase-separated poly(A)-binding protein (Pab1) by its cognate disaggregation systemF31ES030697 · NIEHS · UNIVERSITY OF CHICAGO · PI YOO, HANEUL · 2019 to 2020
$91k
NIEHS NIH HHS F31 ES030697NIGMS NIH HHS R01 GM126547NIGMS NIH HHS R01 GM127406NIGMS NIH HHS R35 GM144278NIGMS NIH HHS T32 GM007183
6 · The paper itself

Abstract

Stresses such as heat shock trigger the formation of protein aggregates and the induction of a disaggregation system composed of molecular chaperones. Recent work reveals that several cases of apparent heat-induced aggregation, long thought to be the result of toxic misfolding, instead reflect evolved, adaptive biomolecular condensation, with chaperone activity contributing to condensate regulation. Here we show that the yeast disaggregation system directly disperses heat-induced biomolecular condensates of endogenous poly(A)-binding protein (Pab1) orders of magnitude more rapidly than aggregates of the most commonly used misfolded model substrate, firefly luciferase. Beyond its efficiency, heat-induced condensate dispersal differs from heat-induced aggregate dispersal in its molecular requirements and mechanistic behavior. Our work establishes a bona fide endogenous heat-induced substrate for long-studied heat shock proteins, isolates a specific example of chaperone regulation of condensates, and underscores needed expansion of the proteotoxic interpretation of the heat shock response to encompass adaptive, chaperone-mediated regulation.

Indexed as

Heat-Shock ResponseBinding, CompetitiveBiomolecular CondensatesHeat-Shock ProteinsHSP40 Heat-Shock ProteinsHSP70 Heat-Shock ProteinsPoly(A)-Binding ProteinsProtein AggregatesProtein BindingProtein FoldingSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsHeat-Shock ProteinsHsP104 protein, S cerevisiaeHSP40 Heat-Shock ProteinsHSP70 Heat-Shock Proteinspab1 protein, S cerevisiaePoly(A)-Binding ProteinsProtein AggregatesSaccharomyces cerevisiae Proteinsbiomolecular condensatescell stressdisaggregationheat shockmolecular chaperonesstress response

Identifiers

PMID35148816
PMCPMC8857057
OpenAlexW4220896612

What OpenQuestion holds

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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.