Evidence map›Paper›PMID 38233718›Full record

ArticleEMBO reports2024

Decoding the function of Atg13 phosphorylation reveals a role of Atg11 in bulk autophagy initiation.

Anuradha Bhattacharya, Raffaela Torggler, Wolfgang Reiter, Natalie Romanov, Mariya Licheva, Akif Ciftci, Muriel Mari, Lena Kolb, Dominik Kaiser, Fulvio Reggiori and 3 more

Open access · diamondAbstract read
In one paragraph

Article in EMBO reports, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
6citing papers in PubMed, 1 pooled it
4.3field-weighted citation impact, top 6% 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

6 citing papers in PubMed, 1 synthesis or guideline pooled it, 11 citations in OpenAlex.

  1. Pooled it
  2. Review
  3. Article
  4. Review
  5. Article
  6. 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

13 authors at 5 institutions in 3 countries.

Anuradha BhattacharyaInstitute of Biochemistry and Molecular Biology, ZBMZ, Faculty of Medicine, University of Freiburg, 79104, Freiburg, Germany.
Raffaela TorgglerInstitute of Biochemistry and Molecular Biology, ZBMZ, Faculty of Medicine, University of Freiburg, 79104, Freiburg, Germany.
Wolfgang ReiterDepartment for Biochemistry and Cell Biology, University of Vienna, Center for Molecular Biology, Vienna Biocenter Campus (VBC), Dr. Bohr-Gasse 9, 1030, Vienna, Austria.ORCID http://orcid.org/0000-0003-1266-8975
Natalie RomanovDepartment for Biochemistry and Cell Biology, University of Vienna, Center for Molecular Biology, Vienna Biocenter Campus (VBC), Dr. Bohr-Gasse 9, 1030, Vienna, Austria.
Mariya LichevaInstitute of Biochemistry and Molecular Biology, ZBMZ, Faculty of Medicine, University of Freiburg, 79104, Freiburg, Germany.ORCID http://orcid.org/0000-0001-7722-7340
Akif CiftciInstitute of Biochemistry and Molecular Biology, ZBMZ, Faculty of Medicine, University of Freiburg, 79104, Freiburg, Germany.
Muriel MariDepartment of Biomedicine, Aarhus University, Ole Worms Allé 4, 8000, Aarhus C, Denmark.ORCID http://orcid.org/0000-0002-2677-6945
Lena KolbDepartment for Biochemistry and Cell Biology, University of Vienna, Center for Molecular Biology, Vienna Biocenter Campus (VBC), Dr. Bohr-Gasse 9, 1030, Vienna, Austria.
Dominik KaiserInstitute of Biochemistry and Molecular Biology, ZBMZ, Faculty of Medicine, University of Freiburg, 79104, Freiburg, Germany.
Fulvio ReggioriDepartment of Biomedicine, Aarhus University, Ole Worms Allé 4, 8000, Aarhus C, Denmark.ORCID http://orcid.org/0000-0003-2652-2686
Gustav AmmererDepartment for Biochemistry and Cell Biology, University of Vienna, Center for Molecular Biology, Vienna Biocenter Campus (VBC), Dr. Bohr-Gasse 9, 1030, Vienna, Austria.
David M HollensteinInstitute of Biochemistry and Molecular Biology, ZBMZ, Faculty of Medicine, University of Freiburg, 79104, Freiburg, Germany. david.hollenstein@univie.ac.at.ORCID http://orcid.org/0000-0002-1977-1556
Claudine KraftInstitute of Biochemistry and Molecular Biology, ZBMZ, Faculty of Medicine, University of Freiburg, 79104, Freiburg, Germany. kraft@biochemie.uni-freiburg.de.ORCID http://orcid.org/0000-0002-3324-4701
University of Freiburg · DEAarhus University · DKVienna Biocenter · ATMax Perutz Labs · ATMax Planck Institute of Biophysics · DE

Funding

Austrian Science Fund (FWF) Special Research Program F34Deutsche Forschungsgemeinschaft (DFG) 259130777Deutsche Forschungsgemeinschaft (DFG) 390939984Deutsche Forschungsgemeinschaft (DFG) 403222702Deutsche Forschungsgemeinschaft (DFG) 409673687EC | European Research Council (ERC) 769065EC | Horizon 2020 Framework Programme (H2020) 765912ENW KLEIN-1 OCENW.KLEIN.118HSRD VA HIR 10-001Novo Nordisk Fonden (NNF) 0066384SNF | Swiss National Centre of Competence in Research Kidney Control of Homeostasis (NCCR Kidney.CH) CRSII5_189952Vienna Science and Technology Fund (WWTF) VRG10-001ZonMW TOP 91217002
6 · The paper itself

Abstract

Autophagy is initiated by the assembly of multiple autophagy-related proteins that form the phagophore assembly site where autophagosomes are formed. Atg13 is essential early in this process, and a hub of extensive phosphorylation. How these multiple phosphorylations contribute to autophagy initiation, however, is not well understood. Here we comprehensively analyze the role of phosphorylation events on Atg13 during nutrient-rich conditions and nitrogen starvation. We identify and functionally characterize 48 in vivo phosphorylation sites on Atg13. By generating reciprocal mutants, which mimic the dephosphorylated active and phosphorylated inactive state of Atg13, we observe that disrupting the dynamic regulation of Atg13 leads to insufficient or excessive autophagy, which are both detrimental to cell survival. We furthermore demonstrate an involvement of Atg11 in bulk autophagy even during nitrogen starvation, where it contributes together with Atg1 to the multivalency that drives phase separation of the phagophore assembly site. These findings reveal the importance of post-translational regulation on Atg13 early during autophagy initiation, which provides additional layers of regulation to control bulk autophagy activity and integrate cellular signals.

Indexed as

AutophagySaccharomyces cerevisiae ProteinsAutophagy-Related ProteinsNitrogenPhosphorylationSignal TransductionAutophagy-Related ProteinsNitrogenSaccharomyces cerevisiae ProteinsAtg11Atg13Atg1 Kinase ComplexAutophagyPAS Formation

Identifiers

PMID38233718
PMCPMC10897315
OpenAlexW4390942706

What OpenQuestion holds

Textmetadata
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.