Evidence map›Paper›PMID 37672657›Full record

ArticleThe Journal of cell biology2023

The RasGAP-associated endoribonuclease G3BP mediates stress granule assembly.

Hélène Tourrière, Karim Chebli, Latifa Zekri, Brice Courselaud, Jean Marie Blanchard, Edouard Bertrand, Jamal Tazi

Open access · bronzeAbstract read
In one paragraph

Article in The Journal of cell biology, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 33 papers.

0numbers the graph read from it
0cells of the map it votes in
33citing papers in PubMed
6.5field-weighted citation impact, top 3% 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

33 citing papers in PubMed, 42 citations in OpenAlex.

  1. Review
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  4. Prion-Like Protein LENG8-Mediated Nucleation Drives Stress Granule Assembly.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026
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  19. Genome-Wide Identification ofPlants (Basel, Switzerland) · 2025
    Article
  20. Aldolase-regulated G3BP1/2The EMBO journal · 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 at 1 institution in 1 country.

Hélène Tourrière *Institut de Génétique Moléculaire de Montpellier, UMR 5535 du Centre National de la Recherche Scientifique (CNRS), Université Montpellier, Montpellier, France.
Karim Chebli *Institut de Génétique Moléculaire de Montpellier, UMR 5535 du Centre National de la Recherche Scientifique (CNRS), Université Montpellier, Montpellier, France.
Latifa ZekriInstitut de Génétique Moléculaire de Montpellier, UMR 5535 du Centre National de la Recherche Scientifique (CNRS), Université Montpellier, Montpellier, France.ORCID 0000-0003-0889-8241
Brice CourselaudInstitut de Génétique Moléculaire de Montpellier, UMR 5535 du Centre National de la Recherche Scientifique (CNRS), Université Montpellier, Montpellier, France.
Jean Marie BlanchardInstitut de Génétique Moléculaire de Montpellier, UMR 5535 du Centre National de la Recherche Scientifique (CNRS), Université Montpellier, Montpellier, France.
Edouard BertrandInstitut de Génétique Moléculaire de Montpellier, UMR 5535 du Centre National de la Recherche Scientifique (CNRS), Université Montpellier, Montpellier, France.ORCID 0000-0002-9642-7994
Jamal TaziInstitut de Génétique Moléculaire de Montpellier, UMR 5535 du Centre National de la Recherche Scientifique (CNRS), Université Montpellier, Montpellier, France.ORCID 0000-0002-1949-8748
Centre National de la Recherche Scientifique · FR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Stress granules (SGs) are formed in the cytoplasm in response to various toxic agents and are believed to play a critical role in the regulation of mRNA metabolism during stress. In SGs, mRNAs are stored in an abortive translation initiation complex that can be routed to either translation initiation or degradation. Here, we show that G3BP, a phosphorylation-dependent endoribonuclease that interacts with RasGAP, is recruited to SGs in cells exposed to arsenite. G3BP may thus determine the fate of mRNAs during cellular stress. Remarkably, SG assembly can be either dominantly induced by G3BP overexpression, or on the contrary, inhibited by expressing a central domain of G3BP. This region binds RasGAP and contains serine 149 whose dephosphorylation is induced by arsenite treatment. Critically, a non-phosphorylatable G3BP mutant (S149A) oligomerizes and assembles SG. These results suggest that G3BP is an effector of SG assembly and that Ras signaling contributes to this process by regulating G3BP dephosphorylation.

Indexed as

Endoribonucleasesras GTPase-Activating ProteinsStress GranulesArsenitesGTPase-Activating ProteinsRNA, MessengerarseniteArsenitesEndoribonucleasesGTPase-Activating Proteinsras GTPase-Activating ProteinsRNA, Messenger

Identifiers

PMID37672657
PMCPMC10482220
OpenAlexW4386469770

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-SA
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.