Elucidation of the Far3- and Far7-mediated regulatory mechanism of mitochondrial autophagy in yeast

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This study investigates mitophagy, which maintains mitochondrial quality and quantity. The Far complex interacts with a receptor protein Atg32 to facilitate mitophagy by phosphorylating it. However, the mechanism of this interaction is still unclear. The study found that Far3/7 do not directly interact with Atg32, but they are needed for Far8-Atg32 interaction. Substitution mutants of Far3/7 phosphorylation sites, expression, degradation, and a set of kinases involved in autophagy did not influence the Atg32-Far complex interaction. The study suggests exploring other known interacting partners of the Far complex and Atg32 and investigating the role of other post-translational modifications, as well as the effect of cellular stress and nutrient availability on the Atg32-Far8 interaction.