Reference: Kubota M and Okamoto K (2021) The protein N-terminal acetyltransferase A complex contributes to yeast mitophagy via promoting expression and phosphorylation of Atg32. J Biochem 170(2):175-182

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Abstract


Mitophagy is an evolutionarily conserved catabolic process that selectively degrades damaged or superfluous mitochondria via autophagy. Although mitophagy is considered to be critical to maintain cellular homeostasis, detailed mechanisms of mitophagy remain largely unknown. In the budding yeast Saccharomyces cerevisiae, the protein N-terminal acetyltransferase A (NatA) complex is important for transcriptional induction of the pro-mitophagic factor Atg32 and efficient degradation of mitochondria under prolonged respiratory conditions. Overexpression of Atg32 only partially recovers mitophagy in cells lacking NatA, raising the possibility that NatA may contribute to mitophagy via additional mechanisms. Here, we demonstrate that Atg32 phosphorylation, which is required for facilitating mitophagy, is altered in respiring NatA-deficient cells. Hyperphosphorylation of Atg32 partially rescues mitophagy in cells lacking NatA. Notably, mitophagy is mostly restored in NatA-null cells overexpressing hyperphosphorylated Atg32. Loss of NatA does not impair the interaction of phosphorylated Atg32 with Atg11, a scaffold protein critical for selective autophagy, suggesting that NatA-dependent Atg32 phosphorylation promotes mitophagy independently of Atg32-Atg11 interactions. We propose that NatA-mediated protein N-terminal acetylation acts in Atg32 expression and phosphorylation to drive mitophagy.

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Journal Article
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Kubota M, Okamoto K
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