Evidence map›Paper›PMID 33893802›Full record

ArticleNucleic acids research2021

eIF4E3 forms an active eIF4F complex during stresses (eIF4FS) targeting mTOR and re-programs the translatome.

Benjamin Weiss, George Edward Allen, Joachim Kloehn, Karim Abid, Pascale Jaquier-Gubler, Joseph Alphonsus Curran

Open access · goldAbstract read
In one paragraph

Article in Nucleic acids research, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.

0numbers the graph read from it
0cells of the map it votes in
20citing papers in PubMed
1.9field-weighted citation impact, top 14% 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

20 citing papers in PubMed, 34 citations in OpenAlex.

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  17. Dysregulated proteostasis network in neuronal diseases.Frontiers in cell and developmental biology · 2023
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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

6 authors at 2 institutions in 1 country.

Benjamin WeissDepartment of Microbiology and Molecular Medicine, Faculty of Medicine, University of Geneva, Switzerland.ORCID 0000-0002-9084-9264
George Edward AllenDepartment of Microbiology and Molecular Medicine, Faculty of Medicine, University of Geneva, Switzerland.
Joachim KloehnDepartment of Microbiology and Molecular Medicine, Faculty of Medicine, University of Geneva, Switzerland.
Karim AbidCatecholamine and Peptides Laboratory, Service of Clinical Pharmacology, Lausanne University Hospital and University of Lausanne, Switzerland.
Pascale Jaquier-GublerDepartment of Microbiology and Molecular Medicine, Faculty of Medicine, University of Geneva, Switzerland.
Joseph Alphonsus CurranDepartment of Microbiology and Molecular Medicine, Faculty of Medicine, University of Geneva, Switzerland.ORCID 0000-0003-4853-440X
University of Geneva · CHUniversity of Lausanne · CH

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The eIF4E are a family of initiation factors that bind the mRNA 5' cap, regulating the proteome and the cellular phenotype. eIF4E1 mediates global translation and its activity is controlled via the PI3K/AKT/mTOR pathway. mTOR down-regulation results in eIF4E1 sequestration into an inactive complex with the 4E binding proteins (4EBPs). The second member, eIF4E2, regulates the translatome during hypoxia. However, the exact function of the third member, eIF4E3, has remained elusive. We have dissected its function using a range of techniques. Starting from the observation that it does not interact with 4EBP1, we demonstrate that eIF4E3 recruitment into an eIF4F complex occurs when Torin1 inhibits the mTOR pathway. Ribo-seq studies demonstrate that this complex (eIF4FS) is translationally active during stress and that it selects specific mRNA populations based on 5' TL (UTR) length. The interactome reveals that it associates with cellular proteins beyond the cognate initiation factors, suggesting that it may have 'moon-lighting' functions. Finally, we provide evidence that cellular metabolism is altered in an eIF4E3 KO background but only upon Torin1 treatment. We propose that eIF4E3 acts as a second branch of the integrated stress response, re-programming the translatome to promote 'stress resistance' and adaptation.

Indexed as

Protein BiosynthesisAnimalsCells, CulturedEukaryotic Initiation Factor-4EEukaryotic Initiation Factor-4FEukaryotic Initiation FactorsHumansMiceNaphthyridinesRNA CapsStress, PhysiologicalTOR Serine-Threonine Kinases1-(4-(4-propionylpiperazin-1-yl)-3-(trifluoromethyl)phenyl)-9-(quinolin-3-yl)benzo(h)(1,6)naphthyridin-2(1H)-oneeIF4E3 protein, humanEukaryotic Initiation Factor-4EEukaryotic Initiation Factor-4FEukaryotic Initiation FactorsNaphthyridinesRNA CapsTOR Serine-Threonine Kinases

Identifiers

PMID33893802
PMCPMC8136781
OpenAlexW3155693148

What OpenQuestion holds

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Registered trials

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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.