Okamoto K~Ohsumi Y, 2009

Pubmed ID 19619494
Title Mitochondria-anchored receptor Atg32 mediates degradation of mitochondria via selective autophagy.
Authors Koji Okamoto, Noriko Kondo-Okamoto, Yoshinori Ohsumi
Abstract Mitochondria are essential organelles that produce most of the energy for a cell, but concomitantly accumulate oxidative damage. Degradation of damaged mitochondria is critical for cell homeostasis, and this process is thought to be mediated by mitophagy, an autophagy-related pathway specific for mitochondria. However, whether mitochondria are selectively degraded, and how the autophagic machinery is targeted to mitochondria, remain largely unknown. Here we demonstrate that, in post-log phase cells under respiratory conditions, a substantial fraction of mitochondria are exclusively sequestered as cargoes and transported to the vacuole, a lytic compartment in yeast, in an autophagy-dependent manner. Interestingly, we found Atg32, a mitochondria-anchored protein essential for mitophagy that is induced during respiratory growth. In addition, our data suggest that Atg32 interacts with Atg8 and Atg11, autophagy-related proteins critical for recognition of cargo receptors. We propose that Atg32 acts as a mitophagy-specific receptor and regulates selective degradation of mitochondria.
Citation Dev. Cell 2009; 17:87-97
Data abstract Deletion collection was screened for strains defective in mitophagy.


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Paper Phenotype Condition Medium Collection Tested mutants Data Details
Okamoto K~Ohsumi Y, 2009 mitophagy (Su9-GFP) standard SGlyCA hap a ~5,150 Discrete

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