Evidence map›Paper›PMID 36354155›Full record

ArticleAutophagy2023

--Atg9 interactions via its transmembrane domains are required for phagophore expansion during autophagy.

Sabrina Chumpen Ramirez, Rubén Gómez-Sánchez, Pauline Verlhac, Ralph Hardenberg, Eleonora Margheritis, Katia Cosentino, Fulvio Reggiori, Christian Ungermann

Open access · hybridAbstract read
In one paragraph

Article in Autophagy, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 34 papers.

0numbers the graph read from it
0cells of the map it votes in
34citing papers in PubMed
6.9field-weighted citation impact, top 2% 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

34 citing papers in PubMed, 47 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. Article
  5. Article
  6. Article
  7. ER membrane receptors engage core autophagy machinery to initiate ER-phagy.Proceedings of the National Academy of Sciences of the United States of America · 2026
    Article
  8. Role of N-glycosylation as a determinant of ATG9A conformations and activity.Protein science : a publication of the Protein Society · 2026
    Article
  9. Article
  10. Article
  11. ATG9 inhibitsAutophagy · 2025
    Article
  12. Article
  13. Article
  14. Monitoring Autophagy in Human Aging: Key Cell Models and Insights.Frontiers in bioscience (Landmark edition) · 2025
    Review
  15. Article
  16. Article
  17. Structural basis for lipid transfer by the ATG2A-ATG9A complex.Nature structural & molecular biology · 2025
    Article
  18. Review
  19. Article
  20. Article
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

8 authors at 2 institutions in 3 countries.

Sabrina Chumpen RamirezOsnabrück University, Department of Biology/Chemistry, Biochemistry section, Osnabrück, Germany.ORCID 0000-0002-2697-9304
Rubén Gómez-SánchezDepartment of Biomedical Sciences of Cells and Systems, University of Groningen, University Medical Center Groningen, Groningen, The Netherlands.ORCID 0000-0002-8274-3259
Pauline VerlhacDepartment of Biomedical Sciences of Cells and Systems, University of Groningen, University Medical Center Groningen, Groningen, The Netherlands.ORCID 0000-0002-1059-4645
Ralph HardenbergDepartment of Biomedical Sciences of Cells and Systems, University of Groningen, University Medical Center Groningen, Groningen, The Netherlands.
Eleonora MargheritisOsnabrück University, Department of Biology/Chemistry, Osnabrück, Germany.
Katia CosentinoOsnabrück University, Department of Biology/Chemistry, Osnabrück, Germany.
Fulvio ReggioriDepartment of Biomedical Sciences of Cells and Systems, University of Groningen, University Medical Center Groningen, Groningen, The Netherlands.ORCID 0000-0003-2652-2686
Christian UngermannOsnabrück University, Department of Biology/Chemistry, Biochemistry section, Osnabrück, Germany.ORCID 0000-0003-4331-8695
Osnabrück University · DEUniversity Medical Center Groningen · NL

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

During macroautophagy/autophagy, precursor cisterna known as phagophores expand and sequester portions of the cytoplasm and/or organelles, and subsequently close resulting in double-membrane transport vesicles called autophagosomes. Autophagosomes fuse with lysosomes/vacuoles to allow the degradation and recycling of their cargoes. We previously showed that sequential binding of yeast Atg2 and Atg18 to Atg9, the only conserved transmembrane protein in autophagy, at the extremities of the phagophore mediates the establishment of membrane contact sites between the phagophore and the endoplasmic reticulum. As the Atg2-Atg18 complex transfers lipids between adjacent membranes

Indexed as

AutophagosomesSaccharomyces cerevisiae ProteinsAutophagyAutophagy-Related ProteinsCryoelectron MicroscopyEndoplasmic ReticulumHumansLipidsMembrane ProteinsSaccharomyces cerevisiaeATG2 protein, S cerevisiaeATG9 protein, S cerevisiaeAutophagy-Related ProteinsLipidsMembrane ProteinsSaccharomyces cerevisiae ProteinsAutophagosomelipid transfermembrane contact sitephagophorescramblase

Identifiers

PMID36354155
PMCPMC10241002
OpenAlexW4308666320

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-ND
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.