Evidence map›Paper›PMID 24879146›Full record

ReviewAutophagy2014

ATG13: just a companion, or an executor of the autophagic program?

Sebastian Alers, Sebastian Wesselborg, Björn Stork

Erratum issuedOpen access · hybridAbstract readReview
In one paragraph

Review in Autophagy, 2014. 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 35 papers.

0numbers the graph read from it
0cells of the map it votes in
35citing papers in PubMed
2.6field-weighted citation impact, top 10% 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, 62 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Molecular mechanism on autophagy associated cardiovascular dysfunction inFrontiers in cell and developmental biology · 2025
    Review
  5. Article
  6. Review
  7. Review
  8. Review
  9. MedComm · 2023
    Article
  10. Autophagy coordinates chondrocyte development and early joint formation in zebrafish.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2021
    Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Article
  20. Review
4 · The record

Corrections and comments

  • Erratum issued
5 · Who and what money

Authors and funding

3 authors at 2 institutions in 2 countries.

Sebastian AlersInstitute of Molecular Medicine; Heinrich-Heine-University; Düsseldorf, Germany.
Sebastian WesselborgInstitute of Molecular Medicine; Heinrich-Heine-University; Düsseldorf, Germany.
Björn StorkInstitute of Molecular Medicine; Heinrich-Heine-University; Düsseldorf, Germany.
Institute of Molecular Medicine · INHeinrich Heine University Düsseldorf · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

During the past 20 years, autophagy signaling has entered the main stage of the cell biological theater. Autophagy represents an intracellular degradation process that is involved in both the bulk recycling of cytoplasmic components and the selective removal of organelles, protein aggregates, or intracellular pathogens. The understanding of autophagy has been greatly facilitated by the characterization of the molecular machinery governing this process. In yeast, initiation of autophagy is controlled by the Atg1 kinase complex, which is composed of the Ser/Thr kinase Atg1, the adaptor protein Atg13, and the ternary complex of Atg17-Atg31-Atg29. In vertebrates, the orthologous ULK1 kinase complex contains the Ser/Thr kinase ULK1 and the accessory proteins ATG13, RB1CC1, and ATG101. Among these components, Atg1/ULK1 have gained major attention in the past, i.e., for the identification of upstream regulatory kinases, the characterization of downstream substrates controlling the autophagic flux, or as a druggable target for the modulation of autophagy. However, accumulating data indicate that the function of Atg13/ATG13 has been likely underestimated so far. In addition to ensuring proper Atg1/ULK1 recruitment and activity, this adaptor molecule has been implicated in ULK1-independent autophagy processes. Furthermore, recent data have identified additional binding partners of Atg13/ATG13 besides the components of the Atg1/ULK1 complex, e.g., Atg8 family proteins or acidic phospholipids. Therefore, in this review we will center the spotlight on Atg13/ATG13 and summarize the role that Atg13/ATG13 assumes in the autophagy stage play.

Indexed as

Adaptor Proteins, Signal TransducingAlternative SplicingAnimalsAutophagyAutophagy-Related Protein-1 HomologAutophagy-Related ProteinsBinding SitesCaenorhabditis elegans ProteinsDrosophila ProteinsHumansIntracellular Signaling Peptides and ProteinsModels, BiologicalPhosphorylationProtein KinasesProtein Serine-Threonine KinasesSaccharomyces cerevisiaeAdaptor Proteins, Signal TransducingAtg13 protein, DrosophilaATG13 protein, humanATG13 protein, S cerevisiaeATG1 protein, S cerevisiaeAutophagy-Related Protein-1 HomologAutophagy-Related ProteinsCaenorhabditis elegans ProteinsDrosophila ProteinsIntracellular Signaling Peptides and ProteinsProtein KinasesProtein Serine-Threonine KinasesSaccharomyces cerevisiae ProteinsULK1 protein, humanUNC-51 protein, C elegansATG101ATG13autophagyRB1CC1ULK1

Identifiers

PMID24879146
PMCPMC4091178
OpenAlexW2324772025

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.