Evidence map›Paper›PMID 23219485›Full record

ArticleCell2012

Architecture of the Atg17 complex as a scaffold for autophagosome biogenesis.

Michael J Ragusa, Robin E Stanley, James H Hurley

Abstract read
In one paragraph

Article in Cell, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 140 papers, 2 of them syntheses that pooled it.

0numbers the graph read from it
0cells of the map it votes in
140citing papers in PubMed, 2 pooled it
–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

140 citing papers in PubMed, 2 syntheses or guidelines pooled it.

  1. Guideline
  2. Guideline
  3. Article
  4. Core principles of autophagy initiation mechanisms.Nature structural & molecular biology · 2026
    Review
  5. Article
  6. The autophagy-specific exocyst subcomplex contributes to phagophore assembly site integrity by promoting phagophore expansion.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  7. Article
  8. The human autophagy-initiating complexes ULK1C and PI3KC3-C1.The Journal of biological chemistry · 2025
    Review
  9. Article
  10. Article
  11. Review
  12. Review
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Article
  20. Review

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

4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

3 authors.

Michael J Ragusa *Laboratory of Molecular Biology, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, MD 20892.
Robin E Stanley *Laboratory of Molecular Biology, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, MD 20892.
James H HurleyLaboratory of Molecular Biology, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, MD 20892.

Funding

Structural mechanisms of autophagyZIADK075067 · NIDDK · NATIONAL INSTITUTE OF DIABETES AND DIGESTIVE AND KIDNEY DISEASES · PI HURLEY, JAMES · 2012 to 2013
$1.8M
The molecular basis for the induction of autophagyF32GM099319 · NIGMS · U.S. NATIONAL INST DIABETES/DIGST/KIDNEY · PI RAGUSA, MICHAEL JOSEPH · 2011 to 2013
$146k
Intramural NIH HHSNIGMS NIH HHS F32 GM099319NIGMS NIH HHS GM099319
6 · The paper itself

Abstract

Macroautophagy is a bulk clearance mechanism in which the double-membraned phagophore grows and engulfs cytosolic material. In yeast, the phagophore nucleates from a cluster of 20-30 nm diameter Atg9-containing vesicles located at a multiprotein assembly known as the preautophagosomal structure (PAS). The crystal structure of a 2:2:2 complex of the earliest acting PAS proteins, Atg17, Atg29, and Atg31, was solved at 3.05 Å resolution. Atg17 is crescent shaped with a 10 nm radius of curvature. Dimerization of the Atg17-Atg31-Atg29 complex is critical for both PAS formation and autophagy, and each dimer contains two separate and complete crescents. Upon induction of autophagy, Atg17-Atg31-Atg29 assembles with Atg1 and Atg13, which in turn initiates the formation of the phagophore. The C-terminal EAT domain of Atg1 was shown to sense membrane curvature, dimerize, and tether lipid vesicles. These data suggest a structural mechanism for the organization of Atg9 vesicles into the early phagophore.

Indexed as

Amino Acid SequenceAutophagyAutophagy-Related ProteinsCarrier ProteinsCrystallography, X-RayFungal ProteinsModels, MolecularMolecular Sequence DataMultiprotein ComplexesPhagosomesProtein Structure, TertiarySaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsSaccharomycetalesSequence AlignmentAtg17 protein, S cerevisiaeAutophagy-Related ProteinsCarrier ProteinsFungal ProteinsMultiprotein ComplexesSaccharomyces cerevisiae Proteins

Identifiers

PMID23219485
PMCPMC3806636

What OpenQuestion holds

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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.