Dec 15, 2020
Association and dissociation between the mitochondrial Far complex and Atg32 regulate mitophagy
eLife
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- Volume
- 9
- Number
- Language
- English
- Publishing type
- Research paper (scientific journal)
- DOI
- 10.7554/elife.63694
- Publisher
- eLife Sciences Publications, Ltd
Mitophagy plays an important role in mitochondrial homeostasis. In yeast, the phosphorylation of the mitophagy receptor Atg32 by casein kinase 2 is essential for mitophagy. This phosphorylation is counteracted by the yeast equivalent of the STRIPAK complex consisting of the PP2A-like protein phosphatase Ppg1 and Far3-7-8-9-10-11 (Far complex), but the underlying mechanism remains elusive. Here we show that two subpopulations of the Far complex reside in the mitochondria and endoplasmic reticulum, respectively, and play distinct roles; the former inhibits mitophagy via Atg32 dephosphorylation, and the latter regulates TORC2 signaling. Ppg1 and Far11 form a subcomplex, and Ppg1 activity is required for the assembling integrity of Ppg1-Far11-Far8. The Far complex preferentially interacts with phosphorylated Atg32, and this interaction is weakened by mitophagy induction. Furthermore, the artificial tethering of Far8 to Atg32 prevents mitophagy. Taken together, the Ppg1-mediated Far complex formation and its dissociation from Atg32 are crucial for mitophagy regulation.
- Link information
- ID information
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- DOI : 10.7554/elife.63694
- eISSN : 2050-084X
- Pubmed ID : 33317697
- Pubmed Central ID : PMC7738187