Evidence map›Paper›PMID 40552710›Full record

ArticleeLife2025

The triad interaction of ULK1, ATG13, and FIP200 is required for ULK complex formation and autophagy.

Yutaro Hama, Yuko Fujioka, Hayashi Yamamoto, Noboru Mizushima, Nobuo N Noda

Abstract read
In one paragraph

Article in eLife, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.

0numbers the graph read from it
0cells of the map it votes in
13citing 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

13 citing papers in PubMed.

  1. Article
  2. Article
  3. Review
  4. Article
  5. Article
  6. Review
  7. Review
  8. Ambiguous Role of p53 in Transcription-Dependent Tumor Cell Death.International journal of molecular sciences · 2026
    Review
  9. Review
  10. Article
  11. Review
  12. Review
  13. ER-driven Contact Sites in Autophagosome Biogenesis Sequence.Contact (Thousand Oaks (Ventura County, Calif.))
    Review
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

5 authors.

Yutaro HamaInstitute for Genetic Medicine, Hokkaido University, Sapporo, Japan.ORCID 0000-0002-7190-4547
Yuko FujiokaInstitute for Genetic Medicine, Hokkaido University, Sapporo, Japan.ORCID 0000-0002-6905-0669
Hayashi YamamotoDepartment of Biochemistry and Molecular Biology, Graduate School of Medicine, The University of Tokyo, Tokyo, Japan.ORCID 0000-0002-2831-1463
Noboru MizushimaDepartment of Biochemistry and Molecular Biology, Graduate School of Medicine, The University of Tokyo, Tokyo, Japan.ORCID 0000-0002-6258-6444
Nobuo N NodaInstitute for Genetic Medicine, Hokkaido University, Sapporo, Japan.ORCID 0000-0002-6940-8069

Funding

Japan Agency for Medical Research and Development JP20gm6410009Japan Science and Technology Agency 10.52926/jpmjcr20e3Japan Science and Technology Agency 10.52926/jpmjer1702Japan Society for the Promotion of Science JP19H05707Japan Society for the Promotion of Science JP21H05256Japan Society for the Promotion of Science JP21H05731Japan Society for the Promotion of Science JP22H04919Japan Society for the Promotion of Science JP22KJ0044Japan Society for the Promotion of Science JP23H02429Japan Society for the Promotion of Science JP23H04923Japan Society for the Promotion of Science JP23K06667Japan Society for the Promotion of Science JP23K14140Japan Society for the Promotion of Science JP23K20044Japan Society for the Promotion of Science JP23K27122Japan Society for the Promotion of Science JP24H00060Japan Society for the Promotion of Science JP25H00966Japan Society for the Promotion of Science JP25H01320Japan Society for the Promotion of Science JP25H01321
6 · The paper itself

Abstract

In mammals, autophagosome formation, a central event in autophagy, is initiated by the ULK complex comprising ULK1/2, FIP200, ATG13, and ATG101. However, the structural basis and mechanism underlying the ULK complex assembly have yet to be fully clarified. Here, we predicted the core interactions organizing the ULK complex using AlphaFold, which proposed that the intrinsically disordered region of ATG13 engages the bases of the two UBL domains in the FIP200 dimer via two phenylalanines and also binds the tandem microtubule-interacting and transport domain of ULK1, thereby yielding the 1:1:2 stoichiometry of the ULK1-ATG13-FIP200 complex. We validated the predicted interactions by point mutations and demonstrated direct triad interactions among ULK1, ATG13, and FIP200 in vitro and in cells, wherein each interaction was additively important for autophagic flux. These results indicate that the ULK1-ATG13-FIP200 triadic interaction is crucial for autophagosome formation and provides a structural basis and insights into the regulation mechanism of autophagy initiation in mammals.

Indexed as

Adaptor Proteins, Signal TransducingAutophagyAutophagy-Related Protein-1 HomologAutophagy-Related ProteinsIntracellular Signaling Peptides and ProteinsAnimalsAutophagosomesHEK293 CellsHumansProtein BindingAdaptor Proteins, Signal TransducingATG13 protein, humanAutophagy-Related Protein-1 HomologAutophagy-Related ProteinsIntracellular Signaling Peptides and ProteinsRB1CC1 protein, humanULK1 protein, humanAlphaFoldATG13autophagycell biologyFIP200humanULK complex

Identifiers

PMID40552710
PMCPMC12187132

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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.