Evidence map›Paper›PMID 32515645›Full record

ArticleAutophagy2021

Atg21 organizes Atg8 lipidation at the contact of the vacuole with the phagophore.

Lena Munzel, Piotr Neumann, Florian B Otto, Roswitha Krick, Janina Metje-Sprink, Benjamin Kroppen, Narain Karedla, Jörg Enderlein, Michael Meinecke, Ralf Ficner and 1 more

Open access · bronzeAbstract read
In one paragraph

Article in Autophagy, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.

0numbers the graph read from it
0cells of the map it votes in
23citing papers in PubMed
2.9field-weighted citation impact, top 9% 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

23 citing papers in PubMed, 38 citations in OpenAlex.

  1. Article
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  3. Full length TECPR1 displays 'cis' Dysferlin domain architecture.bioRxiv : the preprint server for biology · 2026
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  6. Review
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  8. Article
  9. Exosome-Autophagy Crosstalk in Enveloped Virus Infection.International journal of molecular sciences · 2023
    Review
  10. Article
  11. Article
  12. Review
  13. Article
  14. Review
  15. Review
  16. Article
  17. Review
  18. Molecular regulation of autophagosome formation.Biochemical Society transactions · 2022
    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

11 authors at 2 institutions in 1 country.

Lena MunzelDepartment of Cellular Biochemistry, University Medicine, Goettingen, Germany.
Piotr NeumannDepartment of Molecular Structural Biology, Institute for Microbiology and Genetics, University of Goettingen, Goettingen, Germany.ORCID 0000-0003-0129-8112
Florian B OttoDepartment of Cellular Biochemistry, University Medicine, Goettingen, Germany.
Roswitha KrickDepartment of Cellular Biochemistry, University Medicine, Goettingen, Germany.
Janina Metje-SprinkDepartment of Neurobiology, Max Planck Institute for Biophysical Chemistry, Goettingen, Germany.ORCID 0000-0002-7168-2606
Benjamin KroppenDepartment of Cellular Biochemistry, University Medicine, Goettingen, Germany.
Narain KaredlaPhysics Department III, University of Goettingen, Goettingen, Germany.ORCID 0000-0002-7891-3825
Jörg EnderleinPhysics Department III, University of Goettingen, Goettingen, Germany.ORCID 0000-0001-5091-7157
Michael MeineckeDepartment of Cellular Biochemistry, University Medicine, Goettingen, Germany.ORCID 0000-0003-1414-6951
Ralf FicnerDepartment of Molecular Structural Biology, Institute for Microbiology and Genetics, University of Goettingen, Goettingen, Germany.ORCID 0000-0002-1739-6086
Michael ThummDepartment of Cellular Biochemistry, University Medicine, Goettingen, Germany.
University of Göttingen · DEMax Planck Institute for Biophysical Chemistry · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Coupling of Atg8 to phosphatidylethanolamine is crucial for the expansion of the crescent-shaped phagophore during cargo engulfment. Atg21, a PtdIns3P-binding beta-propeller protein, scaffolds Atg8 and its E3-like complex Atg12-Atg5-Atg16 during lipidation. The crystal structure of Atg21, in complex with the Atg16 coiled-coil domain, showed its binding at the bottom side of the Atg21 beta-propeller. Our structure allowed detailed analyses of the complex formation of Atg21 with Atg16 and uncovered the orientation of the Atg16 coiled-coil domain with respect to the membrane. We further found that Atg21 was restricted to the phagophore edge, near the vacuole, known as the vacuole isolation membrane contact site (VICS). We identified a specialized vacuolar subdomain at the VICS, typical of organellar contact sites, where the membrane protein Vph1 was excluded, while Vac8 was concentrated. Furthermore, Vac8 was required for VICS formation. Our results support a specialized organellar contact involved in controlling phagophore elongation.

Indexed as

AutophagosomesAutophagyAutophagy-Related Protein 8 FamilyAutophagy-Related ProteinsEndopeptidasesMicrotubule-Associated ProteinsSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsVacuolesATG21 protein, S cerevisiaeATG8 protein, S cerevisiaeAutophagy-Related Protein 8 FamilyAutophagy-Related ProteinsEndopeptidasesMicrotubule-Associated ProteinsSaccharomyces cerevisiae ProteinsAtg16Atg21Atg8 lipidationorganellar contact sitephagophore elongationVICS

Identifiers

PMID32515645
PMCPMC8205015
OpenAlexW3033533743

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.