Evidence map›Paper›PMID 30258106›Full record

ArticleScientific reports2018

A short isoform of ATG7 fails to lipidate LC3/GABARAP.

M H Ogmundsdottir, V Fock, L Sooman, V Pogenberg, R Dilshat, C Bindesbøll, H M Ogmundsdottir, A Simonsen, M Wilmanns, E Steingrimsson

Erratum issuedOpen access · goldAbstract read
In one paragraph

Article in Scientific reports, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 11 papers, 2 of them syntheses that pooled it.

0numbers the graph read from it
0cells of the map it votes in
11citing papers in PubMed, 2 pooled it
0.8field-weighted citation impact, top 26% 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

11 citing papers in PubMed, 2 syntheses or guidelines pooled it, 12 citations in OpenAlex.

  1. Pooled it
  2. Guideline
  3. Article
  4. Article
  5. Review
  6. Article
  7. Review
  8. ATG7 is a haploinsufficient repressor of tumor progression and promoter of metastasis.Proceedings of the National Academy of Sciences of the United States of America · 2022
    Article
  9. Article
  10. Review
  11. Article
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

10 authors at 3 institutions in 3 countries.

M H OgmundsdottirDepartment of Biochemistry and Molecular Biology, Biomedical Center, Faculty of Medicine, University of Iceland, Sturlugata 8, 101, Reykjavik, Iceland. mho@hi.is.
V FockDepartment of Biochemistry and Molecular Biology, Biomedical Center, Faculty of Medicine, University of Iceland, Sturlugata 8, 101, Reykjavik, Iceland.
L SoomanDepartment of Biochemistry and Molecular Biology, Biomedical Center, Faculty of Medicine, University of Iceland, Sturlugata 8, 101, Reykjavik, Iceland.
V PogenbergEuropean Molecular Biology Laboratory, Hamburg Unit, Notkestrasse 85, 22607, Hamburg, Germany.
R DilshatDepartment of Biochemistry and Molecular Biology, Biomedical Center, Faculty of Medicine, University of Iceland, Sturlugata 8, 101, Reykjavik, Iceland.
C BindesbøllDepartment of Molecular Medicine, Institute of Basic Medical Sciences, University of Oslo, Sognsvannsveien 9, N-0317, Oslo, Norway.
H M OgmundsdottirCancer Research Laboratory, Biomedical Center, Faculty of Medicine, University of Iceland, Sturlugata 8, 101, Reykjavik, Iceland.
A SimonsenDepartment of Molecular Medicine, Institute of Basic Medical Sciences, University of Oslo, Sognsvannsveien 9, N-0317, Oslo, Norway.
M WilmannsEuropean Molecular Biology Laboratory, Hamburg Unit, Notkestrasse 85, 22607, Hamburg, Germany.
E SteingrimssonDepartment of Biochemistry and Molecular Biology, Biomedical Center, Faculty of Medicine, University of Iceland, Sturlugata 8, 101, Reykjavik, Iceland. eirikurs@hi.is.
University of Iceland · ISEuropean Molecular Biology Laboratory · DEUniversity of Oslo · NO

Funding

Austrian Science Fund FWF J 3864
6 · The paper itself

Abstract

Autophagy is a degradation pathway important for cellular homeostasis. The E1-like enzyme ATG7 is a key component of the autophagy machinery, with the main function of mediating the lipidation of LC3/GABARAP during autophagosome formation. By analysing mRNA-sequencing data we found that in addition to the full-length ATG7 isoform, various tissues express a shorter isoform lacking an exon of 27 amino acids in the C-terminal part of the protein, termed ATG7(2). We further show that ATG7(2) does not bind LC3B and fails to mediate the lipidation of members of the LC3/GABARAP family. We have thus identified an isoform of ATG7 that is unable to carry out the best characterized function of the protein during the autophagic response. This short isoform will have to be taken into consideration when further studying the role of ATG7.

Indexed as

Adaptor Proteins, Signal TransducingAmino Acid SequenceAnimalsApoptosis Regulatory ProteinsAutophagyAutophagy-Related Protein 7HEK293 CellsHumansLipid MetabolismMiceMicrotubule-Associated ProteinsModels, MolecularProtein BindingProtein IsoformsAdaptor Proteins, Signal TransducingApoptosis Regulatory ProteinsATG7 protein, humanAutophagy-Related Protein 7GABARAP protein, humanMAP1LC3B protein, humanMicrotubule-Associated ProteinsProtein Isoforms

Identifiers

PMID30258106
PMCPMC6158294
OpenAlexW2889864666

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.