@phdthesis{oai:niigata-u.repo.nii.ac.jp:02000296,
 author = {Innokentev, Aleksei and インノケンチエフ, アレクセイ},
 month = {2022-04-04, 2022-04-04},
 note = {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., eLife. 2020, 9, e63694., 新大院博(医)第991号},
 school = {新潟大学, Niigata University},
 title = {Association and dissociation between the mitochondrial Far complex and Atg32 regulate mitophagy},
 year = {}
}