Evidence map›Paper›PMID 25658430›Full record

ArticlePLoS pathogens2015

Viral and cellular proteins containing FGDF motifs bind G3BP to block stress granule formation.

Marc D Panas, Tim Schulte, Bastian Thaa, Tatiana Sandalova, Nancy Kedersha, Adnane Achour, Gerald M McInerney

Open access · goldAbstract read
In one paragraph

Article in PLoS pathogens, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 107 papers.

0numbers the graph read from it
0cells of the map it votes in
107citing papers in PubMed
6.9field-weighted citation impact, top 2% 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

107 citing papers in PubMed, 159 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Review
  5. Article
  6. Pharmacological modulation of stress granulesFrontiers in pharmacology · 2026
    Review
  7. Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Review
  15. Article
  16. Article
  17. Article
  18. Article
  19. Article
  20. Stress granule formation helps to mitigate neurodegeneration.bioRxiv : the preprint server for biology · 2023
    Article

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

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 3 institutions in 2 countries.

Marc D PanasDepartment of Microbiology, Tumor and Cell Biology, Karolinska Institutet, Stockholm, Sweden.
Tim SchulteScience for Life Laboratory, Department of Medicine Solna, Karolinska Institutet, Stockholm, Sweden.
Bastian ThaaDepartment of Microbiology, Tumor and Cell Biology, Karolinska Institutet, Stockholm, Sweden.
Tatiana SandalovaScience for Life Laboratory, Department of Medicine Solna, Karolinska Institutet, Stockholm, Sweden.
Nancy KedershaDivision of Rheumatology, Immunology and Allergy, Brigham and Women's Hospital, Boston, Massachusetts, United States of America.
Adnane AchourScience for Life Laboratory, Department of Medicine Solna, Karolinska Institutet, Stockholm, Sweden.
Gerald M McInerneyDepartment of Microbiology, Tumor and Cell Biology, Karolinska Institutet, Stockholm, Sweden.
Karolinska Institutet · SEScience for Life Laboratory · SEBrigham and Women's Hospital · US

Funding

Angiogenin-Induced RNA Cleavage in CancerR01CA168872 · NCI · BRIGHAM AND WOMEN'S HOSPITAL · PI ANDERSON, PAUL J. · 2013 to 2015
$1.1M
Characterization of mammalian stress granulesR56AI033600 · NIAID · BRIGHAM AND WOMEN'S HOSPITAL · PI ANDERSON, PAUL J. · 2005 to 2005
$437k
NCI NIH HHS R01 CA168872NIAID NIH HHS R56 AI033600
6 · The paper itself

Abstract

The Ras-GAP SH3 domain-binding proteins (G3BP) are essential regulators of the formation of stress granules (SG), cytosolic aggregates of proteins and RNA that are induced upon cellular stress, such as virus infection. Many viruses, including Semliki Forest virus (SFV), block SG induction by targeting G3BP. In this work, we demonstrate that the G3BP-binding motif of SFV nsP3 consists of two FGDF motifs, in which both phenylalanine and the glycine residue are essential for binding. In addition, we show that binding of the cellular G3BP-binding partner USP10 is also mediated by an FGDF motif. Overexpression of wt USP10, but not a mutant lacking the FGDF-motif, blocks SG assembly. Further, we identified FGDF-mediated G3BP binding site in herpes simplex virus (HSV) protein ICP8, and show that ICP8 binding to G3BP also inhibits SG formation, which is a novel function of HSV ICP8. We present a model of the three-dimensional structure of G3BP bound to an FGDF-containing peptide, likely representing a binding mode shared by many proteins to target G3BP.

Indexed as

Carrier ProteinsDNA-Binding ProteinsHerpesvirus 1, HumanModels, MolecularViral ProteinsAmino Acid MotifsAnimalsCell LineCricetinaeCytoplasmic GranulesDNA HelicasesHumansPoly-ADP-Ribose Binding ProteinsProtein BindingRNA HelicasesRNA Recognition Motif ProteinsCarrier ProteinsDNA-Binding ProteinsDNA HelicasesG3BP1 protein, humanICP8 protein, SimplexvirusPoly-ADP-Ribose Binding ProteinsRNA HelicasesRNA Recognition Motif ProteinsViral Proteins

Identifiers

PMID25658430
PMCPMC4450067
OpenAlexW2063594656

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.