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Aup1p, a Yeast Mitochondrial Protein Phosphatase Homolog, Is Required for Efficient Stationary Phase Mitophagy and Cell Survival
Open accessAbstract
Autophagy is a catabolic membrane-trafficking process that occurs in all eukaryotic cells and leads to the hydrolytic degradation of cytosolic material in the vacuolar or lysosomal lumen. Mitophagy, a selective form of autophagy targeting mitochondria, is poorly understood at present. Several recent reports suggest that mitophagy is a selective process that targets damaged mitochondria, whereas other studies imply a role for mitophagy in cell death processes. In a screen for protein phosphatase homologs that functionally interact with the autophagy-dedicated protein kinase Atg1p in yeast, we have identified Aup1p, encoded by Saccharomyces cerevisiae reading frame YCR079w. Aup1p is highly similar to a family of protein phosphatase homologs in animal cells that are predicted to localize to mitochondria based on sequence analysis. Interestingly, we found that Aup1p localizes to the mitochondrial intermembrane space and is required for efficient mitophagy in stationary phase cells. Viability studies demonstrate that Aup1p is required for efficient survival of cells in prolonged stationary phase cultures, implying a pro-survival role for mitophagy under our working conditions. Our data suggest that Aup1p may be part of a signal transduction mechanism that marks mitochondria for sequestration into autophagosomes.
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“Involvement in mitophagy was also demonstrated in S. cerevisiae for the mitochondrial type 2C protein phosphatase encoded by PTC6 (AUP1) (Tal et al. 2007; Journo et al. 2009), which is also a retrograde target in C. albicans.”
From Mitochondrial retrograde control of transcription evolves with respiratory stress, metabolic adaptation, and virulence in budding yeasts (2026) · cites this paper as Tal et al. 2007
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“In addition, mitophagy can also be induced by culturing the cells in a nonfermentable carbon source to postlog phase.”
From Guidelines for the use and interpretation of assays for monitoring autophagy (2012) · cites this paper as [517]
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Metadata
- Authors
- Tal, R., Winter, G., Ecker, N., Klionsky, D. J., & Abeliovich, H.
- Affiliations
- Hebrew University of Jerusalem (IL)
- University of Michigan (US)
- Corresponding author
- Abeliovich, Hagai
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 2007-02
- Volume
- 282
- Issue
- 8
- Pages
- 5617-5624
- ISSN
- 0021-9258 (ISSN-L)
- OpenAlex
- W1968016394
- Cited by
- 268
- References
- 51
- Citations by year
- 2026: 3 · 2025: 4 · 2024: 9 · 2023: 4 · 2022: 8 · 2021: 17 · 2020: 5 · 2019: 11 · 2018: 11 · 2017: 12 · 2016: 18 · 2015: 12 · 2014: 15 · 2013: 20 · 2012: 26
- FWCI
- 11.22
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- Locations
- Journal of Biological Chemistry (publishedVersion, cc-by)
- PubMed (publishedVersion)
- EPubDev Repository (submittedVersion)
- RUNE (Research UNE) (submittedVersion)
- Funders
- National Institute of General Medical Sciences (GM 53396, R01GM053396)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Autophagy in Disease and Therapy
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Fungal and yeast genetics research
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Ubiquitin and proteasome pathways
- Keywords
- mitophagy, autophagy, stationary phase, cell survival, mitochondrial intermembrane space, autophagosome formation, mitochondrial targeting, signal transduction, Saccharomyces cerevisiae
- MeSH terms
- Autophagy-Related Proteins, Autophagy, Mitochondria, Phosphoprotein Phosphatases, Protein Kinases, Saccharomyces cerevisiae, Mitochondrial Proteins, Saccharomyces cerevisiae Proteins
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