Evidence map›Paper›PMID 24025448›Full record

ArticleAutophagy2013

Proteolytic processing of Atg32 by the mitochondrial i-AAA protease Yme1 regulates mitophagy.

Ke Wang, Meiyan Jin, Xu Liu, Daniel J Klionsky

Abstract read
In one paragraph

Article in Autophagy, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 43 papers.

0numbers the graph read from it
0cells of the map it votes in
43citing papers in PubMed
–field-weighted citation impact
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

43 citing papers in PubMed.

  1. Molecular mechanisms of mitochondrial AAA+ proteases.The Journal of biological chemistry · 2026
    Review
  2. Article
  3. Review
  4. Article
  5. Review
  6. Article
  7. Article
  8. Article
  9. Review
  10. Review
  11. Article
  12. Review
  13. Review
  14. Article
  15. Yeast mitophagy: Unanswered questions.Biochimica et biophysica acta. General subjects · 2021
    Review
  16. Common Principles and Specific Mechanisms of Mitophagy from Yeast to Humans.International journal of molecular sciences · 2021
    Review
  17. Review
  18. Plant Mitophagy in Comparison to Mammals: What Is Still Missing?International journal of molecular sciences · 2021
    Review
  19. Article
  20. Mitophagy: An Emerging Role in Aging and Age-Associated Diseases.Frontiers in cell and developmental biology · 2020
    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

4 authors.

Ke WangLife Sciences Institute and Department of Molecular, Cellular and Developmental Biology; University of Michigan; Ann Arbor, MI USA.
Meiyan Jin
Xu Liu
Daniel J Klionsky

Funding

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

Abstract

Mitophagy, the autophagic removal of mitochondria, occurs through a highly selective mechanism. In the yeast Saccharomyces cerevisiae, the mitochondrial outer membrane protein Atg32 confers selectivity for mitochondria sequestration as a cargo by the autophagic machinery through its interaction with Atg11, a scaffold protein for selective types of autophagy. The activity of mitophagy in vivo must be tightly regulated considering that mitochondria are essential organelles that produce most of the cellular energy, but also generate reactive oxygen species that can be harmful to cell physiology. We found that Atg32 was proteolytically processed at its C terminus upon mitophagy induction. Adding an epitope tag to the C terminus of Atg32 interfered with its processing and caused a mitophagy defect, suggesting the processing is required for efficient mitophagy. Furthermore, we determined that the mitochondrial i-AAA protease Yme1 mediated Atg32 processing and was required for mitophagy. Finally, we found that the interaction between Atg32 and Atg11 was significantly weakened in yme1∆ cells. We propose that the processing of Atg32 by Yme1 acts as an important regulatory mechanism of cellular mitophagy activity.

Indexed as

MitophagyProteolysisATP-Dependent ProteasesAutophagy-Related ProteinsMitochondriaMolecular WeightProtein BindingReceptors, Cytoplasmic and NuclearSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsVesicular Transport ProteinsAtg11 protein, S cerevisiaeAtg32 protein, S cerevisiaeATP-Dependent ProteasesAutophagy-Related ProteinsReceptors, Cytoplasmic and NuclearSaccharomyces cerevisiae ProteinsVesicular Transport ProteinsYME1 protein, S cerevisiaemitochondrial proteasemitophagystarvationvacuoleyeast

Identifiers

PMID24025448
PMCPMC4028336

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.