Evidence map›Paper›PMID 25139988›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2014

Assembly and dynamics of the autophagy-initiating Atg1 complex.

Goran Stjepanovic, Christopher W Davies, Robin E Stanley, Michael J Ragusa, Do Jin Kim, James H Hurley

Open access · bronzeAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 50 papers.

0numbers the graph read from it
0cells of the map it votes in
50citing papers in PubMed
5.4field-weighted citation impact, top 4% 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

50 citing papers in PubMed, 78 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Review
  5. Article
  6. Omic AI reveals new autophagy regulators from the Atg1 interactome inFrontiers in cell and developmental biology · 2025
    Article
  7. Article
  8. Article
  9. Review
  10. Article
  11. Article
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  13. Article
  14. Review
  15. Review
  16. Article
  17. Lighting up Nobel Prize-winning studies with protein intrinsic disorder.Cellular and molecular life sciences : CMLS · 2022
    Review
  18. Article
  19. Review
  20. Molecular regulation of autophagosome formation.Biochemical Society transactions · 2022
    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

6 authors at 3 institutions in 1 country.

Goran StjepanovicDepartment of Molecular and Cell Biology and California Institute for Quantitative Biosciences, University of California, Berkeley, CA 94720; and.
Christopher W DaviesDepartment of Molecular and Cell Biology and California Institute for Quantitative Biosciences, University of California, Berkeley, CA 94720; and.
Robin E StanleyLaboratory of Molecular Biology, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, MD 20892.
Michael J RagusaDepartment of Molecular and Cell Biology and California Institute for Quantitative Biosciences, University of California, Berkeley, CA 94720; and Laboratory of Molecular Biology, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, MD 20892.
Do Jin KimDepartment of Molecular and Cell Biology and California Institute for Quantitative Biosciences, University of California, Berkeley, CA 94720; and.
James H HurleyDepartment of Molecular and Cell Biology and California Institute for Quantitative Biosciences, University of California, Berkeley, CA 94720; and jimhurley@berkeley.edu.
University of California, Berkeley · USQB3 · USNational Institute of Diabetes and Digestive and Kidney Diseases · US

Funding

The Autophagy Initiation ComplexesR01GM111730 · NIGMS · UNIVERSITY OF CALIFORNIA BERKELEY · PI HURLEY, JAMES H · 2014 to 2021
$2.2M
The molecular basis for the induction of autophagyF32GM099319 · NIGMS · U.S. NATIONAL INST DIABETES/DIGST/KIDNEY · PI RAGUSA, MICHAEL JOSEPH · 2011 to 2013
$146k
Mechanism for the Regulation of Starvation-Induced AutophagyF32GM112301 · NIGMS · UNIVERSITY OF CALIFORNIA BERKELEY · PI DAVIES, CHRISTOPHER WILLIAMSON · 2014 to 2014
$50k
NIGMS NIH HHS F32 GM099319NIGMS NIH HHS F32 GM112301NIGMS NIH HHS GM099319NIGMS NIH HHS GM111730NIGMS NIH HHS GM112301NIGMS NIH HHS R01 GM111730
6 · The paper itself

Abstract

The autophagy-related 1 (Atg1) complex of Saccharomyces cerevisiae has a central role in the initiation of autophagy following starvation and TORC1 inactivation. The complex consists of the protein kinase Atg1, the TORC1 substrate Atg13, and the trimeric Atg17-Atg31-Atg29 scaffolding subcomplex. Autophagy is triggered when Atg1 and Atg13 assemble with the trimeric scaffold. Here we show by hydrogen-deuterium exchange coupled to mass spectrometry that the mutually interacting Atg1 early autophagy targeting/tethering domain and the Atg13 central domain are highly dynamic in isolation but together form a stable complex with ∼ 100-nM affinity. The Atg1-Atg13 complex in turn binds as a unit to the Atg17-Atg31-Atg29 scaffold with ∼ 10-μM affinity via Atg13. The resulting complex consists primarily of a dimer of pentamers in solution. These results lead to a model for autophagy initiation in which Atg1 and Atg13 are tightly associated with one another and assemble transiently into the pentameric Atg1 complex during starvation.

Indexed as

Adaptor Proteins, Signal TransducingAmino Acid SequenceAutophagyAutophagy-Related ProteinsCalorimetryCarrier ProteinsCrystallography, X-RayGene DeletionMolecular Sequence DataMultiprotein ComplexesProtein BindingProtein KinasesProtein Structure, QuaternarySaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsAdaptor Proteins, Signal TransducingATG13 protein, S cerevisiaeAtg17 protein, S cerevisiaeATG1 protein, S cerevisiaeATG29 protein, S cerevisiaeAtg31 protein, S cerevisiaeAutophagy-Related ProteinsCarrier ProteinsMultiprotein ComplexesProtein KinasesSaccharomyces cerevisiae Proteinsanalytical ultracentrifugationintrinsically disordered proteinsisothermal titration calorimetrymembrane tetheringprotein structure

Identifiers

PMID25139988
PMCPMC4156731
OpenAlexW2072746398

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.