Evidence map›Paper›PMID 33274589›Full record

ArticleEMBO reports2020

Atg1 kinase regulates autophagosome-vacuole fusion by controlling SNARE bundling.

Saskia Barz, Franziska Kriegenburg, Anna Henning, Anuradha Bhattacharya, Hector Mancilla, Pablo Sánchez-Martín, Claudine Kraft

Open access · hybridAbstract read
In one paragraph

Article in EMBO reports, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.

0numbers the graph read from it
0cells of the map it votes in
22citing papers in PubMed
3.9field-weighted citation impact, top 5% 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

22 citing papers in PubMed, 47 citations in OpenAlex.

  1. Article
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  6. Omic AI reveals new autophagy regulators from the Atg1 interactome inFrontiers in cell and developmental biology · 2025
    Article
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  8. Physiological functions of ULK1/2.Journal of molecular biology · 2024
    Review
  9. Article
  10. Review
  11. Article
  12. Article
  13. Article
  14. Yeast Lsm Pro-Apoptotic Mutants Show Defects in Autophagy.International journal of molecular sciences · 2023
    Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Review
  20. Review
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.

Saskia BarzInstitute of Biochemistry and Molecular Biology, ZBMZ, Faculty of Medicine, University of Freiburg, Freiburg, Germany.
Franziska KriegenburgInstitute of Biochemistry and Molecular Biology, ZBMZ, Faculty of Medicine, University of Freiburg, Freiburg, Germany.
Anna HenningInstitute of Biochemistry and Molecular Biology, ZBMZ, Faculty of Medicine, University of Freiburg, Freiburg, Germany.
Anuradha BhattacharyaInstitute of Biochemistry and Molecular Biology, ZBMZ, Faculty of Medicine, University of Freiburg, Freiburg, Germany.
Hector MancillaInstitute of Biochemistry and Molecular Biology, ZBMZ, Faculty of Medicine, University of Freiburg, Freiburg, Germany.
Pablo Sánchez-MartínInstitute of Biochemistry and Molecular Biology, ZBMZ, Faculty of Medicine, University of Freiburg, Freiburg, Germany.
Claudine KraftInstitute of Biochemistry and Molecular Biology, ZBMZ, Faculty of Medicine, University of Freiburg, Freiburg, Germany.ORCID 0000-0002-3324-4701
University of Freiburg · DE

Funding

Deutsche Forschungsgemeinschaft (DFG) 259130777Deutsche Forschungsgemeinschaft (DFG) 403222702Deutsche Forschungsgemeinschaft (DFG) 450216812EC | H2020 | H2020 Priority Excellent Science | H2020 European Research Council (ERC) 769065EC | H2020 | H2020 Priority Excellent Science | H2020 Marie Skłodowska-Curie Actions (MSCA) 765912EMBO Young Investigator 2875
6 · The paper itself

Abstract

Autophagy mediates the degradation of cytoplasmic material. Upon autophagy induction, autophagosomes form a sealed membrane around the cargo and fuse with the lytic compartment to release the cargo for degradation. In order to avoid premature fusion of immature autophagosomal membranes with the lytic compartment, this process needs to be tightly regulated. Several factors mediating autophagosome-vacuole fusion have recently been identified. In budding yeast, autophagosome-vacuole fusion requires the R-SNARE Ykt6 on the autophagosome, together with the three Q-SNAREs Vam3, Vam7, and Vti1 on the vacuole. However, how these SNAREs are regulated during the fusion process is poorly understood. In this study, we investigate the regulation of Ykt6. We found that Ykt6 is directly phosphorylated by Atg1 kinase, which keeps this SNARE in an inactive state. Ykt6 phosphorylation prevents SNARE bundling by disrupting its interaction with the vacuolar SNAREs Vam3 and Vti1, thereby preventing premature autophagosome-vacuole fusion. These findings shed new light on the regulation of autophagosome-vacuole fusion and reveal a further step in autophagy controlled by the Atg1 kinase.

Indexed as

Saccharomyces cerevisiae ProteinsSNARE ProteinsAutophagosomesAutophagyMembrane FusionR-SNARE ProteinsVacuolesR-SNARE ProteinsSaccharomyces cerevisiae ProteinsSNARE ProteinsAtg1autophagosomeautophagySNAREYkt6

Identifiers

PMID33274589
PMCPMC7726815
OpenAlexW3107138217

What OpenQuestion holds

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LicenceCC BY
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.