Evidence map›Paper›PMID 34739333›Full record

ArticleScience (New York, N.Y.)2021

Ubiquitination of G3BP1 mediates stress granule disassembly in a context-specific manner.

Youngdae Gwon, Brian A Maxwell, Regina-Maria Kolaitis, Peipei Zhang, Hong Joo Kim, J Paul Taylor

Open access · greenAbstract read
In one paragraph

Article in Science (New York, N.Y.), 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 205 papers.

0numbers the graph read from it
0cells of the map it votes in
205citing papers in PubMed
18.1field-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

205 citing papers in PubMed, 320 citations in OpenAlex.

  1. Review
  2. Review
  3. Review
  4. Article
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  8. BOULE is Essential for the Dynamic Disassembly of Heat Shock Granules in Male Germ Cells.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026
    Article
  9. Article
  10. Article
  11. Ubiquitination plays a key role in an insecticide resistance fitness cost.Proceedings of the National Academy of Sciences of the United States of America · 2026
    Article
  12. Article
  13. Article
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  15. Article
  16. Article
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  20. Review

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

4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

6 authors at 1 institution in 1 country.

Youngdae GwonDepartment of Cell and Molecular Biology, St. Jude Children's Research Hospital, Memphis, TN, USA.ORCID 0000-0002-5618-9370
Brian A MaxwellDepartment of Cell and Molecular Biology, St. Jude Children's Research Hospital, Memphis, TN, USA.ORCID 0000-0002-0177-3991
Regina-Maria KolaitisDepartment of Cell and Molecular Biology, St. Jude Children's Research Hospital, Memphis, TN, USA.ORCID 0000-0001-9872-6309
Peipei ZhangDepartment of Cell and Molecular Biology, St. Jude Children's Research Hospital, Memphis, TN, USA.
Hong Joo KimDepartment of Cell and Molecular Biology, St. Jude Children's Research Hospital, Memphis, TN, USA.ORCID 0000-0002-9157-1612
J Paul TaylorDepartment of Cell and Molecular Biology, St. Jude Children's Research Hospital, Memphis, TN, USA.ORCID 0000-0002-5794-0349
St. Jude Children's Research Hospital · US

Funding

Dynamic RNA-protein assemblies and neurological diseaseR35NS097974 · NINDS · ST. JUDE CHILDREN'S RESEARCH HOSPITAL · PI TAYLOR, JOSEPH PAUL · 2017 to 2024
$7.2M
Amyotrophic Lateral Sclerosis Association 18-IIA-419Howard Hughes Medical InstituteNIH HHS R35NS097074NINDS NIH HHS R35 NS097974
6 · The paper itself

Abstract

Stress granules are dynamic, reversible condensates composed of RNA and protein that assemble in eukaryotic cells in response to a variety of stressors and are normally disassembled after stress is removed. The composition and assembly of stress granules is well understood, but little is known about the mechanisms that govern disassembly. Impaired disassembly has been implicated in some diseases including amyotrophic lateral sclerosis, frontotemporal dementia, and multisystem proteinopathy. Using cultured human cells, we found that stress granule disassembly was context-dependent: Specifically in the setting of heat shock, disassembly required ubiquitination of G3BP1, the central protein within the stress granule RNA-protein network. We found that ubiquitinated G3BP1 interacted with the endoplasmic reticulum–associated protein FAF2, which engaged the ubiquitin-dependent segregase p97/VCP (valosin-containing protein). Thus, targeting of G3BP1 weakened the stress granule–specific interaction network, resulting in granule disassembly.

Indexed as

Heat-Shock ResponseAutophagyBlood ProteinsCell Line, TumorCytoplasmic GranulesDNA HelicasesEndoplasmic ReticulumHEK293 CellsHumansIntracellular MembranesMembrane ProteinsMutationPoly-ADP-Ribose Binding ProteinsPolyubiquitinProtein DomainsProteolysisBlood ProteinsDNA HelicasesFAF2 protein, humanG3BP1 protein, humanMembrane ProteinsPoly-ADP-Ribose Binding ProteinsPolyubiquitinRNA HelicasesRNA Recognition Motif ProteinsUbiquitinated ProteinsValosin Containing ProteinVCP protein, human

Identifiers

PMID34739333
PMCPMC8574224
OpenAlexW3174904045

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.