Evidence map›Paper›PMID 22456507›Full record

ArticleMolecular biology of the cell2012

Dynamic and transient interactions of Atg9 with autophagosomes, but not membrane integration, are required for autophagy.

A Orsi, M Razi, H C Dooley, D Robinson, A E Weston, L M Collinson, S A Tooze

Abstract read
In one paragraph

Article in Molecular biology of the cell, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 314 papers.

0numbers the graph read from it
0cells of the map it votes in
314citing papers in PubMed
24.9field-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

314 citing papers in PubMed, 567 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. Article
  5. Where and how do mammalian cells shape autophagosomes?The Journal of biological chemistry · 2026
    Review
  6. Article
  7. Role of N-glycosylation as a determinant of ATG9A conformations and activity.Protein science : a publication of the Protein Society · 2026
    Article
  8. Article
  9. Review
  10. Review
  11. Article
  12. Article
  13. Progress on multifunctional transmembrane protein ATG9A.Cell communication and signaling : CCS · 2025
    Review
  14. Article
  15. Review
  16. Article
  17. Article
  18. Review
  19. Article
  20. Article

254 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

7 authors at 1 institution in 1 country.

A OrsiLondon Research Institute, Cancer Research UK, London, United Kingdom.
M Razi
H C Dooley
D Robinson
A E Weston
L M Collinson
S A Tooze
Cancer Research UK · GB

Funding

Cancer Research UK 15153
6 · The paper itself

Abstract

Autophagy is a catabolic process essential for cell homeostasis, at the core of which is the formation of double-membrane organelles called autophagosomes. Atg9 is the only known transmembrane protein required for autophagy and is proposed to deliver membrane to the preautophagosome structures and autophagosomes. We show here that mammalian Atg9 (mAtg9) is required for the formation of DFCP1-positive autophagosome precursors called phagophores. mAtg9 is recruited to phagophores independent of early autophagy proteins, such as ULK1 and WIPI2, but does not become a stable component of the autophagosome membrane. In fact, mAtg9-positive structures interact dynamically with phagophores and autophagosomes without being incorporated into them. The membrane compartment enriched in mAtg9 displays a unique sedimentation profile, which is unaltered upon starvation-induced autophagy. Correlative light electron microscopy reveals that mAtg9 is present on tubular-vesicular membranes emanating from vacuolar structures. We show that mAtg9 resides in a unique endosomal-like compartment and on endosomes, including recycling endosomes, where it interacts with the transferrin receptor. We propose that mAtg9 trafficking through multiple organelles, including recycling endosomes, is essential for the initiation and progression of autophagy; however, rather than acting as a structural component of the autophagosome, it is required for the expansion of the autophagosome precursor.

Indexed as

AutophagyAnimalsAutophagy-Related Protein-1 HomologAutophagy-Related ProteinsBiomarkersCarrier ProteinsGene Knockdown TechniquesHEK293 CellsHumansIntracellular MembranesIntracellular Signaling Peptides and ProteinsMembrane ProteinsMiceMice, KnockoutMicroscopy, FluorescenceMicrotubule-Associated ProteinsATG9A protein, humanAutophagy-Related Protein-1 HomologAutophagy-Related ProteinsBiomarkersCarrier ProteinsIntracellular Signaling Peptides and ProteinsMAP1LC3A protein, humanMembrane ProteinsMicrotubule-Associated ProteinsPhosphate-Binding ProteinsProtein Serine-Threonine KinasesReceptors, TransferrinULK1 protein, humanVesicular Transport ProteinsWIPI2 protein, humanZFYVE1 protein, human

Identifiers

PMID22456507
PMCPMC3350551
OpenAlexW2032186831

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-SA
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.