Evidence map›Paper›PMID 36498892›Full record

ReviewInternational journal of molecular sciences2022

Role of Proteostasis Regulation in the Turnover of Stress Granules.

Rirong Hu, Beituo Qian, Ang Li, Yanshan Fang

Open access · goldAbstract readReview
In one paragraph

Review in International journal of molecular sciences, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.

0numbers the graph read from it
0cells of the map it votes in
12citing papers in PubMed
1.1field-weighted citation impact, top 23% 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

12 citing papers in PubMed, 13 citations in OpenAlex.

  1. BOULE is Essential for the Dynamic Disassembly of Heat Shock Granules in Male Germ Cells.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026
    Article
  2. TSC2 is a stress granule suppressor.bioRxiv : the preprint server for biology · 2026
    Article
  3. Review
  4. Article
  5. Article
  6. Review
  7. Review
  8. Biomolecular condensates and disease pathogenesis.Science China. Life sciences · 2024
    Review
  9. Review
  10. Article
  11. TheActa biochimica et biophysica Sinica · 2023
    Article
  12. 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

4 authors at 2 institutions in 1 country.

Rirong HuInterdisciplinary Research Center on Biology and Chemistry, Shanghai Institute of Organic Chemistry, Chinese Academy of Sciences, Shanghai 201203, China.
Beituo QianInterdisciplinary Research Center on Biology and Chemistry, Shanghai Institute of Organic Chemistry, Chinese Academy of Sciences, Shanghai 201203, China.
Ang LiGuangdong-Hong Kong-Macau Institute of CNS Regeneration, Key Laboratory of CNS Regeneration of Ministry of Education, Jinan University, Guangzhou 510632, China.ORCID 0000-0002-9886-4880
Yanshan FangInterdisciplinary Research Center on Biology and Chemistry, Shanghai Institute of Organic Chemistry, Chinese Academy of Sciences, Shanghai 201203, China.ORCID 0000-0002-4123-0174
Chinese Academy of Sciences · CNJinan University · CN

Funding

National Natural Science Foundation of China 32270812, 31970697National Natural Science Foundation of China 82071372Natural Science Foundation of Guangdong Province 2021A1515011231Outstanding Scholar Program of Bioland Laboratory 2018GZR110102002Science and Technology Commission of Shanghai Municipality 201409003300, 2019SHZDZX02, 20490712600Science and Technology Program of Guangzhou 202007030012
6 · The paper itself

Abstract

RNA-binding proteins (RBPs) and RNAs can form dynamic, liquid droplet-like cytoplasmic condensates, known as stress granules (SGs), in response to a variety of cellular stresses. This process is driven by liquid-liquid phase separation, mediated by multivalent interactions between RBPs and RNAs. The formation of SGs allows a temporary suspension of certain cellular activities such as translation of unnecessary proteins. Meanwhile, non-translating mRNAs may also be sequestered and stalled. Upon stress removal, SGs are disassembled to resume the suspended biological processes and restore the normal cell functions. Prolonged stress and disease-causal mutations in SG-associated RBPs can cause the formation of aberrant SGs and/or impair SG disassembly, consequently raising the risk of pathological protein aggregation. The machinery maintaining protein homeostasis (proteostasis) includes molecular chaperones and co-chaperones, the ubiquitin-proteasome system, autophagy, and other components, and participates in the regulation of SG metabolism. Recently, proteostasis has been identified as a major regulator of SG turnover. Here, we summarize new findings on the specific functions of the proteostasis machinery in regulating SG disassembly and clearance, discuss the pathological and clinical implications of SG turnover in neurodegenerative disorders, and point to the unresolved issues that warrant future exploration.

Indexed as

Cytoplasmic GranulesProteostasisMolecular ChaperonesRNARNA-Binding ProteinsStress GranulesStress, PhysiologicalMolecular ChaperonesRNARNA-Binding ProteinsautophagychaperonesG3BPstress granuleubiquitinUPSVCP

Identifiers

PMID36498892
PMCPMC9741362
OpenAlexW4309715001

What OpenQuestion holds

Textmetadata
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.