Evidence map›Paper›PMID 34798055›Full record

ArticleMolecular cell2021

Multilayered regulation of autophagy by the Atg1 kinase orchestrates spatial and temporal control of autophagosome formation.

Anne Schreiber, Ben C Collins, Colin Davis, Radoslav I Enchev, Angie Sedra, Rocco D'Antuono, Ruedi Aebersold, Matthias Peter

Open access · hybridAbstract read
In one paragraph

Article in Molecular cell, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.

0numbers the graph read from it
0cells of the map it votes in
16citing papers in PubMed
3.0field-weighted citation impact, top 8% 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

16 citing papers in PubMed, 33 citations in OpenAlex.

  1. Article
  2. Review
  3. The Human Autophagy Core Complexes.Annual review of biochemistry · 2026
    Review
  4. Article
  5. Article
  6. Review
  7. Article
  8. Article
  9. Review
  10. Review
  11. Article
  12. Interactome ofInternational journal of molecular sciences · 2023
    Article
  13. Article
  14. Atg8-PE protein-basedAutophagy · 2022
    Review
  15. Molecular regulation of autophagosome formation.Biochemical Society transactions · 2022
    Review
  16. Review
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

8 authors at 3 institutions in 2 countries.

Anne SchreiberCellular Degradation Systems Laboratory, The Francis Crick Institute, 1 Midland Road, NW1 1AT London, UK; Institute of Biochemistry, ETH Zürich, Otto-Stern-Weg 3, 8093 Zürich, Switzerland. Electronic address: anne.schreiber@crick.ac.uk.
Ben C CollinsInstitute of Molecular Systems Biology, ETH Zürich, Otto-Stern-Weg 3, 8093 Zürich, Switzerland; School of Biological Sciences, Queen's University of Belfast, 19 Chlorine Gardens, BT9 5DL Belfast, UK.
Colin DavisCellular Degradation Systems Laboratory, The Francis Crick Institute, 1 Midland Road, NW1 1AT London, UK.
Radoslav I EnchevInstitute of Biochemistry, ETH Zürich, Otto-Stern-Weg 3, 8093 Zürich, Switzerland; Visual Biochemistry Laboratory, The Francis Crick Institute, 1 Midland Road, NW1 1AT London, UK.
Angie SedraInstitute of Biochemistry, ETH Zürich, Otto-Stern-Weg 3, 8093 Zürich, Switzerland.
Rocco D'AntuonoCrick Advanced Light Microscopy (CALM) STP, The Francis Crick Institute, 1 Midland Road, NW1 1AT London, UK.
Ruedi AebersoldInstitute of Molecular Systems Biology, ETH Zürich, Otto-Stern-Weg 3, 8093 Zürich, Switzerland.
Matthias PeterInstitute of Biochemistry, ETH Zürich, Otto-Stern-Weg 3, 8093 Zürich, Switzerland. Electronic address: matthias.peter@bc.biol.ethz.ch.
The Francis Crick Institute · GBETH Zurich · CHQueen's University Belfast · GB

Funding

Cancer Research UKMedical Research CouncilWellcome Trust FC001598
6 · The paper itself

Abstract

Autophagy is a conserved intracellular degradation pathway exerting various cytoprotective and homeostatic functions by using de novo double-membrane vesicle (autophagosome) formation to target a wide range of cytoplasmic material for vacuolar/lysosomal degradation. The Atg1 kinase is one of its key regulators, coordinating a complex signaling program to orchestrate autophagosome formation. Combining in vitro reconstitution and cell-based approaches, we demonstrate that Atg1 is activated by lipidated Atg8 (Atg8-PE), stimulating substrate phosphorylation along the growing autophagosomal membrane. Atg1-dependent phosphorylation of Atg13 triggers Atg1 complex dissociation, enabling rapid turnover of Atg1 complex subunits at the pre-autophagosomal structure (PAS). Moreover, Atg1 recruitment by Atg8-PE self-regulates Atg8-PE levels in the growing autophagosomal membrane by phosphorylating and thus inhibiting the Atg8-specific E2 and E3. Our work uncovers the molecular basis for positive and negative feedback imposed by Atg1 and how opposing phosphorylation and dephosphorylation events underlie the spatiotemporal regulation of autophagy.

Indexed as

AutophagyAdaptor Proteins, Signal TransducingAutophagosomesAutophagy-Related Protein 8 FamilyAutophagy-Related ProteinsEnzyme ActivationGene Expression Regulation, EnzymologicGene Expression Regulation, FungalPhosphorylationProtein KinasesSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsSignal TransductionTime FactorsAdaptor Proteins, Signal TransducingATG13 protein, S cerevisiaeATG1 protein, S cerevisiaeATG8 protein, S cerevisiaeAutophagy-Related Protein 8 FamilyAutophagy-Related ProteinsProtein KinasesSaccharomyces cerevisiae ProteinsAtg8 lipidationautophagymetabolismphosphorylationprotein kinasesprotein phosphatasessignalingubiquitin-like proteins

Identifiers

PMID34798055
PMCPMC8693860
OpenAlexW3211928633

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.