Evidence map›Paper›PMID 32009292›Full record

ArticleEMBO reports2020

A conserved ATG2-GABARAP family interaction is critical for phagophore formation.

Mihaela Bozic, Luuk van den Bekerom, Beth A Milne, Nicola Goodman, Lisa Roberston, Alan R Prescott, Thomas J Macartney, Nina Dawe, David G McEwan

Open access · hybridAbstract read
In one paragraph

Article in EMBO reports, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 68 papers.

0numbers the graph read from it
0cells of the map it votes in
68citing papers in PubMed
15.3field-weighted citation impact, top 1% 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

68 citing papers in PubMed, 104 citations in OpenAlex.

  1. Regulation and roles of mammalian mitophagy.Nature reviews. Molecular cell biology · 2026
    Review
  2. Article
  3. Article
  4. Review
  5. Article
  6. Article
  7. Review
  8. Review
  9. Article
  10. Ceramide and the membrane-fusion activity of LC3/GABARAP autophagy proteins.Cellular and molecular life sciences : CMLS · 2025
    Article
  11. Review
  12. Article
  13. Article
  14. Article
  15. Article
  16. Review
  17. Review
  18. Structural basis for lipid transfer by the ATG2A-ATG9A complex.Nature structural & molecular biology · 2025
    Article
  19. Review
  20. Review

8 more citing papers are in PubMed but not listed here.

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

9 authors at 1 institution in 1 country.

Mihaela Bozic *Division of Cell Signalling & Immunology, School of Life Sciences, University of Dundee, Dundee, UK.
Luuk van den Bekerom *Division of Cell Signalling & Immunology, School of Life Sciences, University of Dundee, Dundee, UK.ORCID 0000-0002-4954-7408
Beth A MilneDivision of Cell Signalling & Immunology, School of Life Sciences, University of Dundee, Dundee, UK.
Nicola GoodmanDivision of Cell Signalling & Immunology, School of Life Sciences, University of Dundee, Dundee, UK.
Lisa RoberstonDivision of Cell Signalling & Immunology, School of Life Sciences, University of Dundee, Dundee, UK.
Alan R PrescottDundee Imaging Facility, School of Life Sciences, University of Dundee, Dundee, UK.
Thomas J MacartneyMRC Protein Phosphorylation and Ubiquitylation Unit, School of Life Sciences, University of Dundee, Dundee, UK.
Nina DaweDivision of Cell Signalling & Immunology, School of Life Sciences, University of Dundee, Dundee, UK.
David G McEwanDivision of Cell Signalling & Immunology, School of Life Sciences, University of Dundee, Dundee, UK.ORCID 0000-0003-0353-6532
University of Dundee · GB

Funding

Tenovus Scotland T16/44Wellcome TrustWellcome Trust 202061/Z/16/Z
6 · The paper itself

Abstract

The intracellular trafficking pathway, macroautophagy, is a recycling and disposal service that can be upregulated during periods of stress to maintain cellular homeostasis. An essential phase is the elongation and closure of the phagophore to seal and isolate unwanted cargo prior to lysosomal degradation. Human ATG2A and ATG2B proteins, through their interaction with WIPI proteins, are thought to be key players during phagophore elongation and closure, but little mechanistic detail is known about their function. We have identified a highly conserved motif driving the interaction between human ATG2 and GABARAP proteins that is in close proximity to the ATG2-WIPI4 interaction site. We show that the ATG2A-GABARAP interaction mutants are unable to form and close phagophores resulting in blocked autophagy, similar to ATG2A/ATG2B double-knockout cells. In contrast, the ATG2A-WIPI4 interaction mutant fully restored phagophore formation and autophagy flux, similar to wild-type ATG2A. Taken together, we provide new mechanistic insights into the requirements for ATG2 function at the phagophore and suggest that an ATG2-GABARAP/GABARAP-L1 interaction is essential for phagophore formation, whereas ATG2-WIPI4 interaction is dispensable.

Indexed as

AutophagosomesMembrane ProteinsApoptosis Regulatory ProteinsAutophagyAutophagy-Related ProteinsHumansMicrotubule-Associated ProteinsProtein TransportVesicular Transport ProteinsApoptosis Regulatory ProteinsATG2B protein, humanAutophagy-Related ProteinsGABARAP protein, humanMembrane ProteinsMicrotubule-Associated ProteinsVesicular Transport ProteinsATG2autophagosomeautophagyGABARAPphagophore

Identifiers

PMID32009292
PMCPMC7054675
OpenAlexW3004220263

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.