Evidence map›Paper›PMID 34893607›Full record

ArticleNature communications2021

Spatial control of avidity regulates initiation and progression of selective autophagy.

David M Hollenstein, Mariya Licheva, Nicole Konradi, David Schweida, Hector Mancilla, Muriel Mari, Fulvio Reggiori, Claudine Kraft

Open access · goldAbstract read
In one paragraph

Article in Nature communications, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.

0numbers the graph read from it
0cells of the map it votes in
21citing papers in PubMed
3.3field-weighted citation impact, top 7% 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

21 citing papers in PubMed, 34 citations in OpenAlex.

  1. Review
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  4. Core principles of autophagy initiation mechanisms.Nature structural & molecular biology · 2026
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  20. In situ structural analysis reveals membrane shape transitions during autophagosome formation.Proceedings of the National Academy of Sciences of the United States of America · 2022
    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 3 institutions in 3 countries.

David M Hollenstein *Department of Biochemistry and Cell Biology, Max Perutz Labs, University of Vienna, Vienna BioCenter (VBC), Dr. Bohr-Gasse 9, 1030, Vienna, Austria.ORCID http://orcid.org/0000-0002-1977-1556
Mariya Licheva *Institute of Biochemistry and Molecular Biology, ZBMZ, Faculty of Medicine, University of Freiburg, 79104, Freiburg, Germany.ORCID http://orcid.org/0000-0001-7722-7340
Nicole KonradiInstitute of Biochemistry and Molecular Biology, ZBMZ, Faculty of Medicine, University of Freiburg, 79104, Freiburg, Germany.
David SchweidaDepartment of Biochemistry and Cell Biology, Max Perutz Labs, University of Vienna, Vienna BioCenter (VBC), Dr. Bohr-Gasse 9, 1030, Vienna, Austria.
Hector MancillaInstitute of Biochemistry and Molecular Biology, ZBMZ, Faculty of Medicine, University of Freiburg, 79104, Freiburg, Germany.
Muriel MariDepartment of Biomedical Sciences of Cells & Systems, University of Groningen, University Medical Center Groningen, Groningen, The Netherlands.ORCID http://orcid.org/0000-0002-2677-6945
Fulvio ReggioriDepartment of Biomedical Sciences of Cells & Systems, University of Groningen, University Medical Center Groningen, Groningen, The Netherlands.ORCID http://orcid.org/0000-0003-2652-2686
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 · DEUniversity Medical Center Groningen · NLUniversity of Vienna · AT

Funding

Austrian Science Fund FWF P 25522
6 · The paper itself

Abstract

Autophagosomes form at the endoplasmic reticulum in mammals, and between the vacuole and the endoplasmic reticulum in yeast. However, the roles of these sites and the mechanisms regulating autophagosome formation are incompletely understood. Vac8 is required for autophagy and recruits the Atg1 kinase complex to the vacuole. Here we show that Vac8 acts as a central hub to nucleate the phagophore assembly site at the vacuolar membrane during selective autophagy. Vac8 directly recruits the cargo complex via the Atg11 scaffold. In addition, Vac8 recruits the phosphatidylinositol 3-kinase complex independently of autophagy. Cargo-dependent clustering and Vac8-dependent sequestering of these early autophagy factors, along with local Atg1 activation, promote phagophore assembly site assembly at the vacuole. Importantly, ectopic Vac8 redirects autophagosome formation to the nuclear membrane, indicating that the vacuolar membrane is not specifically required. We propose that multiple avidity-driven interactions drive the initiation and progression of selective autophagy.

Indexed as

MacroautophagyAnimalsAutophagosomesAutophagy-Related ProteinsEndopeptidasesHumansMembrane ProteinsNuclear EnvelopeProtein KinasesSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsVacuolesVesicular Transport ProteinsYeastsATG1 protein, S cerevisiaeATG21 protein, S cerevisiaeAutophagy-Related ProteinsEndopeptidasesMembrane ProteinsProtein KinasesSaccharomyces cerevisiae ProteinsVAC8 protein, S cerevisiaeVesicular Transport Proteins

Identifiers

PMID34893607
PMCPMC8664900
OpenAlexW4200186672

What OpenQuestion holds

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Registered trials

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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.