ArticlePloS one2016
The Degradation Pathway of the Mitophagy Receptor Atg32 Is Re-Routed by a Posttranslational Modification.
Article in PloS one, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.
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Who cites it
15 citing papers in PubMed.
- Yeast mitochondrial adaptation to freeze thaw stress depends on pre freeze fermentation state.NPJ science of food · 2026Article
- Optimized Mechanical Isolation of Mitochondria FromBio-protocol · 2026Article
- Retrograde signaling is required for Slm35-mediated negative regulation of mitophagy in yeast.Biology open · 2026Article
- Review
- Modulating autophagy and mitophagy as a promising therapeutic approach in neurodegenerative disorders.Life sciences · 2022Review
- Degradation Mechanism of Autophagy-Related Proteins and Research Progress.International journal of molecular sciences · 2022Review
- MoWhi2 Mediates Mitophagy to Regulate Conidiation and Pathogenesis inInternational journal of molecular sciences · 2022Article
- Review
- Mitophagy in Yeast: Decades of Research.Cells · 2021Review
- Yeast mitophagy: Unanswered questions.Biochimica et biophysica acta. General subjects · 2021Review
- Article
- Mechanistic Insights into the Role of Atg11 in Selective Autophagy.Journal of molecular biology · 2020Review
- Article
- Mechanisms and Physiological Roles of Mitophagy in Yeast.Molecules and cells · 2018Review
- Interaction between autophagy and senescence is required for dihydroartemisinin to alleviate liver fibrosis.Cell death & disease · 2017Article
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Authors and funding
3 authors.
Funding
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Abstract
The outer mitochondrial membrane protein Atg32 is the central receptor for mitophagy, the mitochondria-specific form of autophagy. Atg32 is an unstable protein, and is rapidly degraded under conditions in which mitophagy is not induced. Here we show that Atg32 undergoes a posttranslational modification upon induction of mitophagy. The modification is dependent on the core autophagic machinery, including Atg8, and on the mitophagy-specific adaptor protein Atg11. The modified Atg32 is targeted to the vacuole where it becomes stabilized when vacuolar proteases are deficient. Interestingly, we find that this degradation pathway differs from the degradation pathway of non-modified Atg32, which neither involves vacuolar proteases, nor the proteasome. These analyses reveal that a posttranslational modification discriminates a form of Atg32 targeting mitochondria for mitophagy from that, which escapes mitophagy by rapid degradation.
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