Evidence map›Paper›PMID 40498985›Full record

ArticleAdvanced science (Weinheim, Baden-Wurttemberg, Germany)2025

Organization of the Proteostasis Network of Membraneless Organelles.

Christine M Lim, Yuqi Bian, Alicia González Díaz, Frank Pun, Alex Zhavoronkov, Richard I Morimoto, Michele Vendruscolo

Abstract read
In one paragraph

Article in Advanced science (Weinheim, Baden-Wurttemberg, Germany), 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it
0cells of the map it votes in
1citing papers in PubMed
–field-weighted citation impact
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

1 citing paper in PubMed.

  1. Organization of the Proteostasis Network of Membraneless Organelles.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2025
    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.

Christine M LimCentre for Misfolding Diseases, Yusuf Hamied Department of Chemistry, University of Cambridge, Cambridge, CB2 1EW, UK.
Yuqi BianCentre for Misfolding Diseases, Yusuf Hamied Department of Chemistry, University of Cambridge, Cambridge, CB2 1EW, UK.
Alicia González DíazCentre for Misfolding Diseases, Yusuf Hamied Department of Chemistry, University of Cambridge, Cambridge, CB2 1EW, UK.
Frank PunInsilico Medicine, Hong Kong Science and Technology Park, Unit 310, 3/F, Building 8W, Phase 2, Science Park, Hong Kong, China.
Alex ZhavoronkovInsilico Medicine, Hong Kong Science and Technology Park, Unit 310, 3/F, Building 8W, Phase 2, Science Park, Hong Kong, China.
Richard I MorimotoDepartment of Biochemistry, Molecular Biology and Cell Biology, Rice Institute for Biomedical Research, Northwestern University, Evanston, IL, 60208-3500, USA.
Michele VendruscoloCentre for Misfolding Diseases, Yusuf Hamied Department of Chemistry, University of Cambridge, Cambridge, CB2 1EW, UK.

Funding

UKRI 10059436UKRI 10061100
6 · The paper itself

Abstract

Membraneless organelles (MLOs) are dynamic macromolecular condensates that act as crucibles to modulate cellular processes. Since MLOs form in the absence of lipid membranes, it is important to understand how their effective regulation is achieved by the protein homeostasis (proteostasis) system. To address this question, a comprehensive mapping of the proteostasis network (PN) of MLOs, comprising over 220 000 protein-protein interactions is reported. This analysis reveals how regulatory proteins (PN proteins) occupy central roles in the overall protein-protein interaction network of MLOs. It is then investigated which branches of the PN are most important in the regulation of MLOs, finding that the anabolic component, which makes up ≈30% of the PN, is more closely involved than the catabolic component, which makes up the remaining ≈70% of the PN. It is also found that translation-related PN proteins and molecular chaperones play central roles in MLO regulation. Finally, how specificity may be achieved despite shared PN components is explored. These findings suggest that HSP70 chaperones function as generic MLO regulators, while client-specific HSP70 co-chaperones confer specificity to the chaperone action. These results identify the composition of the PN of MLOs, rationalize its organization, and reveal central roles of molecular chaperones in protein regulation within MLOs.

Indexed as

OrganellesProteostasisMolecular ChaperonesProtein Interaction MapsMolecular Chaperonesliquid‐liquid phase separationmembraneless organellesprotein condensationprotein homeostasis

Identifiers

PMID40498985
PMCPMC12412463

What OpenQuestion holds

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LicenceCC BY
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.