Evidence map›Paper›PMID 30917996›Full record

ArticleThe Journal of cell biology2019

ATG9A shapes the forming autophagosome through Arfaptin 2 and phosphatidylinositol 4-kinase IIIβ.

Delphine Judith, Harold B J Jefferies, Stefan Boeing, David Frith, Ambrosius P Snijders, Sharon A Tooze

Open access · hybridAbstract read
In one paragraph

Article in The Journal of cell biology, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 118 papers.

0numbers the graph read from it
0cells of the map it votes in
118citing papers in PubMed
18.7field-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

118 citing papers in PubMed, 206 citations in OpenAlex.

  1. Emerging mechanisms of ATG8-independent non-canonical autophagy.Journal of physiology and biochemistry · 2026
    Review
  2. Review
  3. Article
  4. Article
  5. Article
  6. Apolipoproteins L involvement in immunity.Journal of human immunity · 2026
    Review
  7. Review
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Progress on multifunctional transmembrane protein ATG9A.Cell communication and signaling : CCS · 2025
    Review
  15. Article
  16. Article
  17. Review
  18. Article
  19. Article
  20. Article

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

4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

6 authors at 1 institution in 1 country.

Delphine JudithMolecular Cell Biology of Autophagy, The Francis Crick Institute, London, UK.
Harold B J JefferiesMolecular Cell Biology of Autophagy, The Francis Crick Institute, London, UK.
Stefan BoeingBioinformatics and Biostatistics, The Francis Crick Institute, London, UK.ORCID 0000-0003-0495-5659
David FrithProteomics, The Francis Crick Institute, London, UK.
Ambrosius P SnijdersProteomics, The Francis Crick Institute, London, UK.
Sharon A ToozeMolecular Cell Biology of Autophagy, The Francis Crick Institute, London, UK sharon.tooze@crick.ac.uk.ORCID 0000-0002-2182-3116
The Francis Crick Institute · GB

Funding

Cancer Research UK 15153Cancer Research UK FC001187Cancer Research UK FC001999Medical Research Council FC001187Wellcome Trust FC001187Wellcome Trust FC001999
6 · The paper itself

Abstract

ATG9A is a multispanning membrane protein essential for autophagy. Normally resident in Golgi membranes and endosomes, during amino acid starvation, ATG9A traffics to sites of autophagosome formation. ATG9A is not incorporated into autophagosomes but is proposed to supply so-far-unidentified proteins and lipids to the autophagosome. To address this function of ATG9A, a quantitative analysis of ATG9A-positive compartments immunoisolated from amino acid-starved cells was performed. These ATG9A vesicles are depleted of Golgi proteins and enriched in BAR-domain containing proteins, Arfaptins, and phosphoinositide-metabolizing enzymes. Arfaptin2 regulates the starvation-dependent distribution of ATG9A vesicles, and these ATG9A vesicles deliver the PI4-kinase, PI4KIIIβ, to the autophagosome initiation site. PI4KIIIβ interacts with ATG9A and ATG13 to control PI4P production at the initiation membrane site and the autophagic response. PI4KIIIβ and PI4P likely function by recruiting the ULK1/2 initiation kinase complex subunit ATG13 to nascent autophagosomes.

Indexed as

Adaptor Proteins, Signal TransducingAutophagosomesAutophagyAutophagy-Related ProteinsEndosomesHEK293 CellsHumansMembrane ProteinsPhosphatidylinositol PhosphatesPhosphotransferases (Alcohol Group Acceptor)Protein TransportVesicular Transport ProteinsAdaptor Proteins, Signal TransducingARFIP2 protein, humanATG13 protein, humanATG9A protein, humanAutophagy-Related ProteinsMembrane Proteinsphosphatidylinositol 4-phosphatePhosphatidylinositol PhosphatesPhosphotransferases (Alcohol Group Acceptor)PI4KB protein, humanVesicular Transport Proteins

Identifiers

PMID30917996
PMCPMC6504893
OpenAlexW2933225319

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.