Evidence map›Paper›PMID 29712776›Full record

ArticleEMBO reports2018

eIF5A is required for autophagy by mediating ATG3 translation.

Michal Lubas, Lea M Harder, Caroline Kumsta, Imke Tiessen, Malene Hansen, Jens S Andersen, Anders H Lund, Lisa B Frankel

Open access · bronzeAbstract read
In one paragraph

Article in EMBO reports, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 59 papers.

0numbers the graph read from it
0cells of the map it votes in
59citing papers in PubMed
7.1field-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

59 citing papers in PubMed, 94 citations in OpenAlex.

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  7. Polyamine Metabolism in Brain Health and Disease.Neuropharmacology and therapy · 2026
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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

8 authors at 3 institutions in 2 countries.

Michal LubasBiotech Research and Innovation Centre, University of Copenhagen, Copenhagen, Denmark.
Lea M HarderDepartment of Biochemistry and Molecular Biology, University of Southern Denmark, Odense, Denmark.
Caroline KumstaProgram of Development, Aging and Regeneration, Sanford Burnham Prebys Medical Discovery Institute, La Jolla, CA, USA.
Imke TiessenBiotech Research and Innovation Centre, University of Copenhagen, Copenhagen, Denmark.
Malene HansenProgram of Development, Aging and Regeneration, Sanford Burnham Prebys Medical Discovery Institute, La Jolla, CA, USA.
Jens S AndersenDepartment of Biochemistry and Molecular Biology, University of Southern Denmark, Odense, Denmark.
Anders H LundBiotech Research and Innovation Centre, University of Copenhagen, Copenhagen, Denmark anders.lund@bric.ku.dk lisa.frankel@bric.ku.dk.ORCID 0000-0002-7407-3398
Lisa B FrankelBiotech Research and Innovation Centre, University of Copenhagen, Copenhagen, Denmark anders.lund@bric.ku.dk lisa.frankel@bric.ku.dk.ORCID 0000-0001-7249-3607
University of Copenhagen · DKSanford Burnham Prebys Medical Discovery Institute · USUniversity of Southern Denmark · DK

Funding

Tumor Microenvironment and Cancer ImmunologyP30CA030199 · NCI · SANFORD BURNHAM PREBYS MEDICAL DISCOVERY INSTITUTE · PI Michael Jackson · 1985 to 2026
$107.2M
Regulation of the Autophagy Process in Organismal AgingR01AG038664 · NIA · SANFORD BURNHAM PREBYS MEDICAL DISCOVERY INSTITUTE · PI Malene Hansen · 2011 to 2026
$6.4M
Autophagy Regulation by Hippo Kinases STK3/STK4R01GM117466 · NIGMS · SANFORD BURNHAM PREBYS MEDICAL DISCOVERY INSTITUTE · PI HANSEN, MALENE · 2016 to 2019
$1.5M
NCI NIH HHS P30 CA030199NIA NIH HHS R01 AG038664NIGMS NIH HHS R01 GM117466
6 · The paper itself

Abstract

Autophagy is an essential catabolic process responsible for recycling of intracellular material and preserving cellular fidelity. Key to the autophagy pathway is the ubiquitin-like conjugation system mediating lipidation of Atg8 proteins and their anchoring to autophagosomal membranes. While regulation of autophagy has been characterized at the level of transcription, protein interactions and post-translational modifications, its translational regulation remains elusive. Here we describe a role for the conserved eukaryotic translation initiation factor 5A (eIF5A) in autophagy. Identified from a high-throughput screen, we find that eIF5A is required for lipidation of LC3B and its paralogs and promotes autophagosome formation. This feature is evolutionarily conserved and results from the translation of the E2-like ATG3 protein. Mechanistically, we identify an amino acid motif in ATG3 causing eIF5A dependency for its efficient translation. Our study identifies eIF5A as a key requirement for autophagosome formation and demonstrates the importance of translation in mediating efficient autophagy.

Indexed as

AutophagyProtein BiosynthesisAutophagosomesAutophagy-Related ProteinsEukaryotic Translation Initiation Factor 5AHumansMCF-7 CellsMicrotubule-Associated ProteinsPeptide Initiation FactorsProtein Processing, Post-TranslationalProteomicsRNA-Binding ProteinsUbiquitin-Conjugating EnzymesATG3 protein, humanAutophagy-Related ProteinsEukaryotic Translation Initiation Factor 5AMAP1LC3B protein, humanMicrotubule-Associated ProteinsPeptide Initiation FactorsRNA-Binding ProteinsUbiquitin-Conjugating EnzymesATG3autophagyeIF5Atranslation

Identifiers

PMID29712776
PMCPMC5989740
OpenAlexW2795455346

What OpenQuestion holds

Textmetadata
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.