Cited by 268Autophagy in Disease and TherapyFungal and yeast genetics researchUbiquitin and proteasome pathways

Aup1p, a yeast mitochondrial protein phosphatase homolog, is required for efficient stationary phase mitophagy and cell survival

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Tal, Ruth, Winter, Gal, Ecker, Nitai, Klionsky, Daniel J., Abeliovich, Hagai·2007·Journal of Biological Chemistry

Abstract

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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Crossref · 10.1074/jbc.m605940200

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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
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
  • Health Sciences › Medicine › Epidemiology › 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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