論文

国際誌
2020年12月15日

Association and dissociation between the mitochondrial Far complex and Atg32 regulate mitophagy

eLife
  • Aleksei Innokentev
  • ,
  • Kentaro Furukawa
  • ,
  • Tomoyuki Fukuda
  • ,
  • Tetsu Saigusa
  • ,
  • Keiichi Inoue
  • ,
  • Shun-ichi Yamashita
  • ,
  • Tomotake Kanki

9
記述言語
英語
掲載種別
研究論文(学術雑誌)
DOI
10.7554/elife.63694
出版者・発行元
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.

リンク情報
DOI
https://doi.org/10.7554/elife.63694
PubMed
https://www.ncbi.nlm.nih.gov/pubmed/33317697
PubMed Central
https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7738187
URL
https://cdn.elifesciences.org/articles/63694/elife-63694-v1.pdf
URL
https://cdn.elifesciences.org/articles/63694/elife-63694-v1.xml
ID情報
  • DOI : 10.7554/elife.63694
  • eISSN : 2050-084X
  • PubMed ID : 33317697
  • PubMed Central 記事ID : PMC7738187

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