Evidence map›Paper›PMID 25998554›Full record

ArticleAutophagy2015

Molecular interactions of the Saccharomyces cerevisiae Atg1 complex provide insights into assembly and regulatory mechanisms.

Leon H Chew, Shan Lu, Xu Liu, Franco Kk Li, Angela Yh Yu, Daniel J Klionsky, Meng-Qiu Dong, Calvin K Yip

Open access · bronzeAbstract read
In one paragraph

Article in Autophagy, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.

0numbers the graph read from it
0cells of the map it votes in
23citing papers in PubMed
2.4field-weighted citation impact, top 12% 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

23 citing papers in PubMed, 36 citations in OpenAlex.

  1. Core principles of autophagy initiation mechanisms.Nature structural & molecular biology · 2026
    Review
  2. Article
  3. Article
  4. A dynamically evolving war between autophagy and pathogenic microorganisms.Journal of Zhejiang University. Science. B · 2022
    Article
  5. Review
  6. Article
  7. Review
  8. Autophagy in Plant Abiotic Stress Management.International journal of molecular sciences · 2021
    Review
  9. Frontiers in cellular and infection microbiology · 2021
    Article
  10. Article
  11. Review
  12. Mechanisms governing autophagosome biogenesis.Nature reviews. Molecular cell biology · 2020
    Review
  13. Article
  14. Review
  15. Review
  16. Frontiers in physiology · 2019
    Article
  17. Article
  18. Article
  19. Article
  20. Next-generation electron microscopy in autophagy research.Current opinion in structural biology · 2016
    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

8 authors at 4 institutions in 4 countries.

Leon H Chewa Department of Biochemistry and Molecular Biology ; University of British Columbia ; Vancouver , BC Canada.
Shan Lu
Xu Liu
Franco Kk Li
Angela Yh Yu
Daniel J Klionsky
Meng-Qiu Dong
Calvin K Yip
University of British Columbia · CANational Institute of Biological Sciences, Beijing · CNLife Science Institute · JPUniversity of Michigan · US

Funding

ALTERNATIVE VACUOLAR TARGETING MECHANISMS IN YEASTR01GM053396 · NIGMS · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI KLIONSKY, DANIEL J. · 1995 to 2018
$12.1M
Canadian Institutes of Health Research MOP-126126NIGMS NIH HHS GM053396NIGMS NIH HHS R01 GM053396
6 · The paper itself

Abstract

The Atg1 complex, which contains 5 major subunits: Atg1, Atg13, Atg17, Atg29, and Atg31, regulates the induction of autophagy and autophagosome formation. To gain a better understanding of the overall architecture and assembly mechanism of this essential autophagy regulatory complex, we have reconstituted a core assembly of the Saccharomyces cerevisiae Atg1 complex composed of full-length Atg17, Atg29, and Atg31, along with the C-terminal domains of Atg1 (Atg1[CTD]) and Atg13 (Atg13[CTD]). Using chemical-crosslinking coupled with mass spectrometry (CXMS) analysis we systematically mapped the intersubunit interaction interfaces within this complex. Our data revealed that the intrinsically unstructured C-terminal domain of Atg29 interacts directly with Atg17, whereas Atg17 interacts with Atg13 in 2 distinct intrinsically unstructured regions, including a previously unknown motif that encompasses several putative phosphorylation sites. The Atg1[CTD] crosslinks exclusively to the Atg13[CTD] and does not appear to make direct contact with the Atg17-Atg31-Atg29 scaffold. Finally, single-particle electron microscopy analysis revealed that both the Atg13[CTD] and Atg1[CTD] localize to the tip regions of Atg17-Atg31-Atg29 and do not alter the distinct curvature of this scaffolding subcomplex. This work provides a comprehensive understanding of the subunit interactions in the fully assembled Atg1 core complex, and uncovers the potential role of intrinsically disordered regions in regulating complex integrity.

Indexed as

Adaptor Proteins, Signal TransducingAutophagyAutophagy-Related ProteinsCarrier ProteinsPhagosomesProtein KinasesSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsAdaptor Proteins, Signal TransducingATG1 protein, S cerevisiaeAutophagy-Related ProteinsCarrier ProteinsProtein KinasesSaccharomyces cerevisiae ProteinsAtg1Atg, autophagy relatedautophagycrosslinking mass spectrometryCTD, C-terminal domainCvt, cytoplasm-to-vacuole targetingCXMS, chemical-crosslinking coupled with mass spectrometryelectron microscopyFDR, false-discovery rateIDR, intrinsically disordered regionmacromolecular assemblyPAS, phagophore assembly sitePtdIns3K, phosphatidylinositol 3-kinaseSaccharomyces cerevisiae

Identifiers

PMID25998554
PMCPMC4502708
OpenAlexW1488820662

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.