ArticleAutophagy2018
A pseudo-receiver domain in Atg32 is required for mitophagy.
Article in Autophagy, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
What it found
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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.
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.
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Who cites it
10 citing papers in PubMed.
- The nascent polypeptide-associated complex subunit Egd1 is required for efficient selective mitochondrial degradation in budding yeast.Scientific reports · 2024Article
- Current opinions on mitophagy in fungi.Autophagy · 2023Review
- Review
- Mitophagy in Yeast: Decades of Research.Cells · 2021Review
- Yeast mitophagy: Unanswered questions.Biochimica et biophysica acta. General subjects · 2021Review
- Common Principles and Specific Mechanisms of Mitophagy from Yeast to Humans.International journal of molecular sciences · 2021Review
- Mitophagy in Human Diseases.International journal of molecular sciences · 2021Review
- Mitophagy Improves Ethanol Tolerance in Yeast: Regulation by Mitochondrial Reactive Oxygen Species inJournal of microbiology and biotechnology · 2020Article
- The Third Coiled Coil Domain of Atg11 Is Required for Shaping Mitophagy Initiation Sites.Journal of molecular biology · 2020Article
- Origin of the Autophagosome Membrane in Mammals.BioMed research international · 2018Review
Corrections and comments
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Authors and funding
6 authors.
Funding
Abstract
Mitochondria are targeted for degradation by mitophagy, a selective form of autophagy. In Saccharomyces cerevisiae, mitophagy is dependent on the autophagy receptor, Atg32, an outer mitochondrial membrane protein. Once activated, Atg32 recruits the autophagy machinery to mitochondria, facilitating mitochondrial capture in phagophores, the precursors to autophagosomes. However, the mechanism of Atg32 activation remains poorly understood. To investigate this crucial step in mitophagy regulation, we examined the structure of Atg32. We have identified a structured domain in Atg32 that is essential for the initiation of mitophagy, as it is required for the proteolysis of the C-terminal domain of Atg32 and the subsequent recruitment of Atg11. The solution structure of this domain was determined by NMR spectroscopy, revealing that Atg32 contains a previously undescribed pseudo-receiver (PsR) domain. Our data suggests that the PsR domain of Atg32 regulates Atg32 activation and the initiation of mitophagy. ABBREVIATIONS:
aimAtg8-interacting motif; GFP: green fluorescent protein; LIR: LC3-interacting region; NMR: nuclear magnetic resonance; NOESY: nuclear Overhauser effect spectroscopy; PDB: protein data bank; PsR: pseudo-receiver; RMSD: root-mean-square deviation.
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What OpenQuestion holds
Registered trials
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.