Journal
CELL REPORTS
Volume 26, Issue 2, Pages 338-+Publisher
CELL PRESS
DOI: 10.1016/j.celrep.2018.12.050
Keywords
-
Categories
Funding
- European Research Council [692659]
- British Heart Foundation [CH/11/3/29051, RG/16/15/32294, RE/13/2/30182]
- Fondation Leducq [RA15CVD04]
- JSPS KAKENHI [18H02807]
- European Research Council (ERC) [692659] Funding Source: European Research Council (ERC)
- Grants-in-Aid for Scientific Research [18H02807] Funding Source: KAKEN
Ask authors/readers for more resources
Degradation of mitochondria by selective autophagy, termed mitophagy, contributes to the control of mitochondrial quality. Bcl2-L-13 is a mammalian homolog of Atg32, which is an essential mitophagy receptor in yeast. However, the molecular machinery involved in Bcl2-L-13-mediated mitophagy remains to be elucidated. Here, we show that the ULK1 (unc-51-like kinase) complex is required for Bcl2-L-13 to process mitophagy. Screening of a series of yeast Atg mutants revealed that a different set of ATG genes is used for Bcl2-L-13- and Atg32-mediated mitophagy in yeast. The components of the Atg1 complex essential for starvation-induced autophagy were indispensable in Bcl2-L-13-, but not Atg32-mediated, mitophagy. The ULK1 complex, a counterpart of the Atg1 complex, is necessary for Bcl2-L-13-mediated mitophagy in mammalian cells. We propose a model where, upon mitophagy induction, Bcl2-L-13 recruits the ULK1 complex to process mitophagy and the interaction of LC3B with ULK1, as well as Bcl2-L-13, is important for the mitophagy.
Authors
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available