Proteolytic processing of Atg32 by the mitochondrial i-AAA protease Yme1 regulates mitophagy.

ABSTRACT: Mitophagy, the autophagic removal of mitochondria, occurs through a highly selective mechanism. In the yeast Saccharomyces cerevisiae, the mitochondrial outer membrane protein Atg32 confers selectivity for mitochondria sequestration as a cargo by the autophagic machinery through its interaction with Atg11, a scaffold protein for selective types of autophagy. The activity of mitophagy in vivo must be tightly regulated considering that mitochondria are essential organelles that produce most of the cellular energy, but also generate reactive oxygen species that can be harmful to cell physiology. We found that Atg32 was proteolytically processed at its C terminus upon mitophagy induction. Adding an epitope tag to the C terminus of Atg32 interfered with its processing and caused a mitophagy def

SUBMITTER: Wang K 

PROVIDER: S-EPMC4028336 | biostudies-literature | 2013 Nov

REPOSITORIES: biostudies-literature