Evidence map›Paper›PMID 33443148›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2021

Downregulation of autophagy by Met30-mediated Atg9 ubiquitination.

Yuchen Feng, Aileen R Ariosa, Ying Yang, Zehan Hu, Jörn Dengjel, Daniel J Klionsky

Open access · greenAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.

0numbers the graph read from it
0cells of the map it votes in
14citing papers in PubMed
2.0field-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

14 citing papers in PubMed, 23 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Review
  10. Article
  11. Degradation Mechanism of Autophagy-Related Proteins and Research Progress.International journal of molecular sciences · 2022
    Review
  12. Review
  13. Article
  14. Autophagy in liver diseases: A review.Molecular aspects of medicine · 2021
    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 2 institutions in 2 countries.

Yuchen FengDepartment of Molecular, Cellular, and Developmental Biology, University of Michigan, Ann Arbor, MI 48109.
Aileen R AriosaLife Sciences Institute, University of Michigan, Ann Arbor, MI 48109.
Ying YangDepartment of Molecular, Cellular, and Developmental Biology, University of Michigan, Ann Arbor, MI 48109.ORCID 0000-0003-1602-1212
Zehan HuDepartment of Biology, University of Fribourg, 1700 Fribourg, Switzerland.
Jörn DengjelDepartment of Biology, University of Fribourg, 1700 Fribourg, Switzerland.ORCID 0000-0002-9453-4614
Daniel J KlionskyDepartment of Molecular, Cellular, and Developmental Biology, University of Michigan, Ann Arbor, MI 48109; klionsky@umich.edu.
University of Michigan · USUniversity of Fribourg · CH

Funding

The mechanism and regulation of autophagyR35GM131919 · NIGMS · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI DANIEL J. KLIONSKY · 2019 to 2026
$6.4M
NIGMS NIH HHS R35 GM131919
6 · The paper itself

Abstract

Macroautophagy/autophagy is a highly conserved eukaryotic molecular process that facilitates the recycling of superfluous cytoplasmic materials, damaged organelles, and invading pathogens, resulting in proper cellular homeostasis and survival during stress conditions. Autophagy is stringently regulated at multiple stages, including control at transcriptional, translational, and posttranslational levels. In this work, we identified a mechanism by which regulation of autophagy is achieved through the posttranslational modification of Atg9. Here, we show that, in order to limit autophagy to a low, basal level during normal conditions, Atg9 is ubiquitinated and subsequently targeted for degradation in a proteasome-dependent manner through the action of the E3 ligase Met30. When cells require increased autophagy flux to respond to nutrient deprivation, the proteolysis of Atg9 is significantly reduced. Overall, this work reveals an additional layer of mechanistic regulation that allows cells to further maintain appropriate levels of autophagy and to rapidly induce this process in response to stress.

Indexed as

AutophagyAutophagy-Related ProteinsDown-RegulationF-Box ProteinsLysosomesMembrane ProteinsProteasome Endopeptidase ComplexProtein Processing, Post-TranslationalProteolysisSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsUbiquitinUbiquitinationUbiquitin-Protein Ligase ComplexesUbiquitin-Protein LigasesATG9 protein, S cerevisiaeAutophagy-Related ProteinsF-Box ProteinsMembrane ProteinsMET30 protein, S cerevisiaeProteasome Endopeptidase ComplexSaccharomyces cerevisiae ProteinsUbiquitinUbiquitin-Protein Ligase ComplexesUbiquitin-Protein Ligasesautophagydegradationlysosomeubiquitinationvacuole

Identifiers

PMID33443148
PMCPMC7817162
OpenAlexW3115150918

What Socratic 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 Socratic graph.