Evidence map›Paper›PMID 30254161›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2018

The Atg2-Atg18 complex tethers pre-autophagosomal membranes to the endoplasmic reticulum for autophagosome formation.

Tetsuya Kotani, Hiromi Kirisako, Michiko Koizumi, Yoshinori Ohsumi, Hitoshi Nakatogawa

Abstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 175 papers, 2 of them syntheses that pooled it.

0numbers the graph read from it
0cells of the map it votes in
175citing 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

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

  1. Stay in touch with the endoplasmic reticulum.Science China. Life sciences · 2024
    Pooled it
  2. Guideline
  3. Review
  4. Article
  5. Article
  6. Article
  7. Functional Homology of WIPI4 and Atg18 EnablesInternational journal of molecular sciences · 2026
    Article
  8. Article
  9. bioRxiv : the preprint server for biology · 2026
    Article
  10. Article
  11. Where and how do mammalian cells shape autophagosomes?The Journal of biological chemistry · 2026
    Review
  12. Article
  13. Core principles of autophagy initiation mechanisms.Nature structural & molecular biology · 2026
    Review
  14. Review
  15. The molecular mechanism of lipid uptake by membrane-anchored bridge-like lipid transfer proteins.Proceedings of the National Academy of Sciences of the United States of America · 2026
    Article
  16. Role of N-glycosylation as a determinant of ATG9A conformations and activity.Protein science : a publication of the Protein Society · 2026
    Article
  17. Review
  18. Article
  19. 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
  20. Review

115 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

5 authors.

Tetsuya KotaniSchool of Life Science and Technology, Tokyo Institute of Technology, Yokohama 226-8501, Japan.
Hiromi KirisakoSchool of Life Science and Technology, Tokyo Institute of Technology, Yokohama 226-8501, Japan.
Michiko KoizumiInstitute of Innovative Research, Tokyo Institute of Technology, Yokohama 226-8503, Japan.
Yoshinori OhsumiInstitute of Innovative Research, Tokyo Institute of Technology, Yokohama 226-8503, Japan.
Hitoshi NakatogawaSchool of Life Science and Technology, Tokyo Institute of Technology, Yokohama 226-8501, Japan; hnakatogawa@bio.titech.ac.jp.ORCID 0000-0002-5828-0741

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The biogenesis of double-membrane vesicles called autophagosomes, which sequester and transport intracellular material for degradation in lysosomes or vacuoles, is a central event in autophagy. This process requires a unique set of factors called autophagy-related (Atg) proteins. The Atg proteins assemble to organize the preautophagosomal structure (PAS), at which a cup-shaped membrane, the isolation membrane (or phagophore), forms and expands to become the autophagosome. The molecular mechanism of autophagosome biogenesis remains poorly understood. Previous studies have shown that Atg2 forms a complex with the phosphatidylinositol 3-phosphate (PI3P)-binding protein Atg18 and localizes to the PAS to initiate autophagosome biogenesis; however, the molecular function of Atg2 remains unknown. In this study, we show that Atg2 has two membrane-binding domains in the N- and C-terminal regions and acts as a membrane tether during autophagosome formation in the budding yeast

Indexed as

AutophagosomesAutophagy-Related ProteinsEndoplasmic ReticulumIntracellular MembranesMembrane ProteinsMultiprotein ComplexesPhosphatidylinositol PhosphatesProtein DomainsSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsATG18 protein, S cerevisiaeATG2 protein, S cerevisiaeAutophagy-Related ProteinsMembrane ProteinsMultiprotein Complexesphosphatidylinositol 3-phosphatePhosphatidylinositol PhosphatesSaccharomyces cerevisiae ProteinsAtg proteinautophagymembrane tetheryeast

Identifiers

PMID30254161
PMCPMC6187169

What OpenQuestion 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 OpenQuestion graph.