The <scp>ESCRT‐III</scp> complex contributes to macromitophagy in yeast

Mitochondria play important roles in energy generation and homeostasis maintenance eukaryotic cells. The damaged or superfluous mitochondria can be nonselectively selectively removed through the autophagy/lysosome pathway, which was referred as mitophagy. According to molecular machinery for degrading mitochondria, occur macromitophagy micromitophagy. In this study, we show that endosomal sorting complex required transport III (ESCRT-III) budding yeast regulates induced by nitrogen starvation, but not post-logarithmic phase growth lactate medium monitoring a mitochondrial marker, Om45. Firstly, loss of ESCRT-III subunit Snf7 Vps4-Vta1 Vps4, two representative subunits ESCRT complex, suppresses delivery degradation Om45-GFP vacuoles. Secondly, marker Om45 mitophagy receptor Atg32 accumulate on autophagosomes marked with Atg8 (mitophagosomes, MPs) mutants. Moreover, protease-protection assay indicates Vps4 are involved MP closure. Finally, interacts Atg11, detected ways, glutathione-S-transferase (GST) pulldown bimolecular fluorescence complementation (BiFC) assay, BiFC interaction happens reticulum. Therefore, proposed mediates starvation-induced between Atg11 so is recruited Atg32-marked MPs known Atg11–Atg32 seal them. These results reveal plays new role macromitophagy.