Evidence map›Paper›PMID 25385507›Full record

ArticleTraffic (Copenhagen, Denmark)2015

Atg23 and Atg27 act at the early stages of Atg9 trafficking in S. cerevisiae.

Steven K Backues, Daniel P Orban, Amélie Bernard, Kushal Singh, Yang Cao, Daniel J Klionsky

Open access · bronzeAbstract read
In one paragraph

Article in Traffic (Copenhagen, Denmark), 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 39 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
39citing 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

39 citing papers in PubMed, 1 synthesis or guideline pooled it, 52 citations in OpenAlex.

  1. Guideline
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Mec1-mediated Atg9 phosphorylation regulates the PAS recruitment of Atg9 vesicles upon energy stress.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  9. Review
  10. Huntingtin contains an ubiquitin-binding domain and regulates lysosomal targeting of mitochondrial and RNA-binding proteins.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  11. Article
  12. Toxics · 2023
    Review
  13. Article
  14. Review
  15. Review
  16. Article
  17. Review
  18. A dynamically evolving war between autophagy and pathogenic microorganisms.Journal of Zhejiang University. Science. B · 2022
    Article
  19. Article
  20. Downregulation of autophagy by Met30-mediated Atg9 ubiquitination.Proceedings of the National Academy of Sciences of the United States of America · 2021
    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

6 authors at 2 institutions in 2 countries.

Steven K BackuesLife Sciences Institute, University of Michigan, Ann Arbor, MI, USA; Current address: Department of Chemistry, Eastern Michigan University, Ypsilanti, MI, USA.
Daniel P Orban
Amélie Bernard
Kushal Singh
Yang Cao
Daniel J Klionsky
University of Michigan–Ann Arbor · USEastern Michigan University · US

Funding

ALTERNATIVE VACUOLAR TARGETING MECHANISMS IN YEASTR01GM053396 · NIGMS · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI KLIONSKY, DANIEL J. · 1995 to 2018
$12.1M
Analysis of Autophagosome FormationF32GM101748 · NIGMS · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI BACKUES, STEVEN KARL · 2012 to 2013
$106k
NIGMS NIH HHS 1-F32-GM-101748-01NIGMS NIH HHS F32 GM101748NIGMS NIH HHS GM053396NIGMS NIH HHS R01 GM053396
6 · The paper itself

Abstract

Atg9 is a conserved multipass transmembrane protein with an essential role in autophagy. In Saccharomyces cerevisiae, it travels through the secretory pathway to a unique compartment, the Atg9 peripheral structures. These structures are then targeted to the phagophore assembly site (PAS), where they are proposed to help deliver membrane to the forming autophagosome. We used 'in vivo reconstitution' of this process in a multiple-knockout strain to define four proteins, Atg11, Atg19, Atg23 and Atg27, as the core minimal machinery necessary and sufficient for the trafficking of Atg9 to the PAS. Atg23 and Atg27 function in the formation of the Atg9 peripheral structures. Overexpression of Atg9 can bypass the need for Atg23, suggesting that the amount of Atg9 in each peripheral structure is a critical factor in their targeting to the PAS. In contrast, overexpression of Atg23 or Atg27 interferes with Atg9 trafficking, suggesting that these proteins must be present in the appropriate stoichiometry in order to function properly. These data allow us to resolve existing controversies regarding the role of Atg23 and Atg27, and propose a model that ties together previous observations regarding the role of Atg9 in autophagosome formation.

Indexed as

Autophagy-Related ProteinsCarrier ProteinsMembrane ProteinsPhagosomesProtein BindingProtein TransportReceptors, Cell SurfaceSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsVesicular Transport ProteinsAtg11 protein, S cerevisiaeATG19 protein, S cerevisiaeAtg23 protein, S cerevisiaeATG27 protein, S cerevisiaeATG9 protein, S cerevisiaeAutophagy-Related ProteinsCarrier ProteinsMembrane ProteinsReceptors, Cell SurfaceSaccharomyces cerevisiae ProteinsVesicular Transport ProteinsautophagyclusteringCvt pathwayGolgiphagophore assembly sitesortingtrafficking

Identifiers

PMID25385507
PMCPMC4305007
OpenAlexW1901455524

What OpenQuestion holds

Textmetadata
LicenceTDM
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.