Evidence map›Paper›PMID 24736843›Full record

ArticleGenes & development2014

Coupling 40S ribosome recruitment to modification of a cap-binding initiation factor by eIF3 subunit e.

Derek Walsh, Ian Mohr

Open access · diamondAbstract read
In one paragraph

Article in Genes & development, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.

0numbers the graph read from it
0cells of the map it votes in
25citing papers in PubMed
–field-weighted citation impact
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

25 citing papers in PubMed, 38 citations in OpenAlex.

  1. Article
  2. Article
  3. Ribosomes in poxvirus infection.Current opinion in virology · 2022
    Review
  4. Article
  5. Review
  6. Article
  7. Article
  8. Article
  9. Article
  10. Translational Control in Cancer.Cold Spring Harbor perspectives in biology · 2019
    Review
  11. Translational control during poxvirus infection.Wiley interdisciplinary reviews. RNA · 2019
    Review
  12. Translational Control in Virus-Infected Cells.Cold Spring Harbor perspectives in biology · 2019
    Review
  13. Article
  14. Review
  15. Review
  16. Article
  17. Article
  18. Article
  19. Article
  20. 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

2 authors at 1 institution in 1 country.

Derek WalshDepartment of Microbiology, New York University School of Medicine, New York, New York 10016, USA.
Ian Mohr
New York University · US

Funding

Control of Translation in Herpesvirus Infected Cells - Resubmission - 1R01GM056927 · NIGMS · NEW YORK UNIVERSITY SCHOOL OF MEDICINE · PI Ian J Mohr · 1999 to 2026
$7.6M
Virus Host Interactions that Regulate Translation in Cells Infected with HSV-1R01AI073898 · NIAID · NEW YORK UNIVERSITY SCHOOL OF MEDICINE · PI MOHR, IAN J · 2008 to 2020
$5.0M
Translational control of gene expression during poxvirus infectionR21AI105330 · NIAID · NORTHWESTERN UNIVERSITY AT CHICAGO · PI WALSH, DEREK · 2014 to 2015
$428k
NIAID NIH HHS R01 AI073898NIAID NIH HHS R01AI073898NIAID NIH HHS R21 AI105330NIAID NIH HHS R21AI105330NIGMS NIH HHS GM056927NIGMS NIH HHS R01 GM056927
6 · The paper itself

Abstract

40S ribosomes are loaded onto capped mRNAs via the multisubunit translation initiation factors eIF3 and eIF4F. While eIF4E is the eIF4F cap recognition component, the eIF4G subunit associates with 40S-bound eIF3. How this intricate process is coordinated remains poorly understood. Here, we identify an eIF3 subunit that regulates eIF4F modification and show that eIF3e is required for inducible eIF4E phosphorylation. Significantly, recruitment of the eIF4E kinase Mnk1 (MAPK signal-integrating kinase 1) to eIF4F depended on eIF3e, and eIF3e was sufficient to promote Mnk1-binding to eIF4G. This establishes a mechanism by which 40S ribosome loading imparts a phosphorylation mark on the cap-binding eIF4F complex that regulates selective mRNA translation and is synchronized by a specific eIF3 subunit.

Indexed as

ChromatographyEukaryotic Initiation Factor-3HumansIntracellular Signaling Peptides and ProteinsPeptide Chain Initiation, TranslationalPhosphorylationProtein BindingProtein Serine-Threonine KinasesProtein SubunitsProtein TransportRibosome Subunits, Small, EukaryoticRNA Cap-Binding ProteinsSignal TransductionEukaryotic Initiation Factor-3Intracellular Signaling Peptides and ProteinsMKNK1 protein, humanProtein Serine-Threonine KinasesProtein SubunitsRNA Cap-Binding ProteinseIF3eIF4E phosphorylationMnk1ribosome recruitmenttranslation initiation

Identifiers

PMID24736843
PMCPMC4003276
OpenAlexW2059617809

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC
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.