Evidence map›Paper›PMID 39174844›Full record

ArticleNature structural & molecular biology2025

Structural basis for lipid transfer by the ATG2A-ATG9A complex.

Yang Wang, Selma Dahmane, Rujuan Ti, Xinyi Mai, Lizhe Zhu, Lars-Anders Carlson, Goran Stjepanovic

Abstract read
PubMed Publisher
In one paragraph

Article in Nature structural & molecular biology, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 37 papers.

0numbers the graph read from it
0cells of the map it votes in
37citing 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

37 citing papers in PubMed.

  1. Article
  2. Article
  3. Article
  4. Regulation and roles of mammalian mitophagy.Nature reviews. Molecular cell biology · 2026
    Review
  5. Article
  6. Review
  7. Article
  8. Article
  9. Review
  10. Article
  11. Review
  12. The Human Autophagy Core Complexes.Annual review of biochemistry · 2026
    Review
  13. Article
  14. Role of N-glycosylation as a determinant of ATG9A conformations and activity.Protein science : a publication of the Protein Society · 2026
    Article
  15. Article
  16. ATG2 is a triglyceride transfer protein.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  17. Article
  18. Article
  19. Article
  20. Article
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

7 authors.

Yang Wang *Kobilka Institute of Innovative Drug Discovery, School of Medicine, The Chinese University of Hong Kong, Shenzhen, Shenzhen, China.ORCID http://orcid.org/0000-0002-3839-0003
Selma Dahmane *Wallenberg Centre for Molecular Medicine, Umeå University, Umeå, Sweden.
Rujuan Ti *Warshel Institute for Computational Biology, The Chinese University of Hong Kong, Shenzhen, Shenzhen, China.ORCID http://orcid.org/0000-0002-5169-8491
Xinyi MaiKobilka Institute of Innovative Drug Discovery, School of Medicine, The Chinese University of Hong Kong, Shenzhen, Shenzhen, China.ORCID http://orcid.org/0009-0004-7828-061X
Lizhe ZhuWarshel Institute for Computational Biology, The Chinese University of Hong Kong, Shenzhen, Shenzhen, China. zhulizhe@cuhk.edu.cn.ORCID http://orcid.org/0000-0001-8252-7807
Lars-Anders CarlsonWallenberg Centre for Molecular Medicine, Umeå University, Umeå, Sweden. lars-anders.carlson@umu.se.ORCID http://orcid.org/0000-0003-2342-6488
Goran StjepanovicKobilka Institute of Innovative Drug Discovery, School of Medicine, The Chinese University of Hong Kong, Shenzhen, Shenzhen, China. goranstjepanovic@cuhk.edu.cn.ORCID http://orcid.org/0000-0002-4841-9949

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Autophagy is characterized by the formation of double-membrane vesicles called autophagosomes. Autophagy-related proteins (ATGs) 2A and 9A have an essential role in autophagy by mediating lipid transfer and re-equilibration between membranes for autophagosome formation. Here we report the cryo-electron microscopy structures of human ATG2A in complex with WD-repeat protein interacting with phosphoinositides 4 (WIPI4) at 3.2 Å and the ATG2A-WIPI4-ATG9A complex at 7 Å global resolution. On the basis of molecular dynamics simulations, we propose a mechanism of lipid extraction from the donor membranes. Our analysis revealed 3:1 stoichiometry of the ATG9A-ATG2A complex, directly aligning the ATG9A lateral pore with ATG2A lipid transfer cavity, and an interaction of the ATG9A trimer with both the N-terminal and the C-terminal tip of rod-shaped ATG2A. Cryo-electron tomography of ATG2A liposome-binding states showed that ATG2A tethers lipid vesicles at different orientations. In summary, this study provides a molecular basis for the growth of the phagophore membrane and lends structural insights into spatially coupled lipid transport and re-equilibration during autophagosome formation.

Indexed as

Autophagy-Related ProteinsMembrane ProteinsVesicular Transport ProteinsAutophagosomesAutophagyCryoelectron MicroscopyHumansLiposomesModels, MolecularMolecular Dynamics SimulationProtein BindingATG2A protein, humanATG9A protein, humanAutophagy-Related ProteinsLiposomesMembrane ProteinsVesicular Transport Proteins

Identifiers

What Socratic 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 Socratic graph.