Evidence map›Paper›PMID 27160682›Full record

ArticleJournal of cell science2016

Sumoylation of eIF4A2 affects stress granule formation.

Jirapas Jongjitwimol, Robert A Baldock, Simon J Morley, Felicity Z Watts

Open access · hybridAbstract read
In one paragraph

Article in Journal of cell science, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 35 papers.

0numbers the graph read from it
0cells of the map it votes in
35citing papers in PubMed
1.6field-weighted citation impact, top 17% 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

35 citing papers in PubMed, 55 citations in OpenAlex.

  1. Review
  2. Review
  3. Article
  4. Article
  5. An HSF1-JMJD6-HSP feedback circuit promotes cell adaptation to proteotoxic stress.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  6. Surface Charge Can Modulate Phase Separation of Multidomain Proteins.Journal of the American Chemical Society · 2024
    Article
  7. Article
  8. Review
  9. Review
  10. Article
  11. Review
  12. Article
  13. Article
  14. Review
  15. Role of the Ubiquitin System in Stress Granule Metabolism.International journal of molecular sciences · 2022
    Review
  16. Review
  17. Review
  18. Review
  19. Article
  20. Molecular mechanisms of stress granule assembly and disassembly.Biochimica et biophysica acta. Molecular cell research · 2021
    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 1 institution in 1 country.

Jirapas JongjitwimolGenome Damage and Stability Centre, School of Life Sciences, University of Sussex, Falmer, Brighton BN1 9RQ, UK.
Robert A BaldockGenome Damage and Stability Centre, School of Life Sciences, University of Sussex, Falmer, Brighton BN1 9RQ, UK.
Simon J MorleyDepartment of Biochemistry and Biomedical Science, School of Life Sciences, University of Sussex, Falmer, Brighton BN1 9QG, UK.
Felicity Z WattsGenome Damage and Stability Centre, School of Life Sciences, University of Sussex, Falmer, Brighton BN1 9RQ, UK f.z.watts@sussex.ac.uk.ORCID 0000-0002-4956-3504
University of Sussex · GB

Funding

Biotechnology and Biological Sciences Research Council BB/H018956/1
6 · The paper itself

Abstract

Regulation of protein synthesis is crucial for cells to maintain viability and to prevent unscheduled proliferation that could lead to tumorigenesis. Exposure to stress results in stalling of translation, with many translation initiation factors, ribosomal subunits and mRNAs being sequestered into stress granules or P bodies. This allows the re-programming of the translation machinery. Many aspects of translation are regulated by post-translational modification. Several proteomic screens have identified translation initiation factors as targets for sumoylation, although in many cases the role of this modification has not been determined. We show here that eIF4A2 is modified by SUMO, with sumoylation occurring on a single residue (K226). We demonstrate that sumoylation of eIF4A2 is modestly increased in response to arsenite and ionising radiation, but decreases in response to heat shock or hippuristanol. In arsenite-treated cells, but not in hippuristanol-treated cells, eIF4A2 is recruited to stress granules, suggesting sumoylation of eIF4A2 correlates with its recruitment to stress granules. Furthermore, we demonstrate that the inability to sumoylate eIF4A2 results in impaired stress granule formation, indicating a new role for sumoylation in the stress response.

Indexed as

Stress, PhysiologicalSumoylationAmino Acid SequenceArsenitesCytoplasmic GranulesEukaryotic Initiation Factor-4AHeat-Shock ResponseHeLa CellsHumansMutationRadiation, IonizingSterolsarseniteArsenitesEukaryotic Initiation Factor-4AhippuristanolSterolsArseniteHeat shockHippuristanolIonising radiationProtein synthesisSUMOTranslation

Identifiers

PMID27160682
PMCPMC4920252
OpenAlexW2345771416

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.