Casein kinase 2 is essential for mitophagy

• Published in: EMBO reports 2013-09, Vol.14 (9), p.788-794
• Main Authors: Kanki, Tomotake, Kurihara, Yusuke, Jin, Xiulian, Goda, Tadahiro, Ono, Yusuke, Aihara, Masamune, Hirota, Yuko, Saigusa, Tetsu, Aoki, Yoshimasa, Uchiumi, Takeshi, Kang, Dongchon
• Format: Article
• Language: English
• Subjects: autophagy; Autophagy-Related Proteins; casein kinase 2; Casein Kinase II - genetics; Casein Kinase II - metabolism; Cellular biology; EMBO31; EMBO37; Kinases; Mitochondria; Mitochondria - metabolism; Mitochondrial Degradation; mitophagy; Molecular biology; Receptors, Cytoplasmic and Nuclear - genetics; Receptors, Cytoplasmic and Nuclear - metabolism; Saccharomyces cerevisiae - enzymology; Saccharomyces cerevisiae - genetics; Saccharomyces cerevisiae - metabolism; Saccharomyces cerevisiae Proteins - genetics; Saccharomyces cerevisiae Proteins - metabolism; Scientific Report; Scientific Reports; Vacuoles - metabolism; Vesicular Transport Proteins - genetics; Vesicular Transport Proteins - metabolism; Yeast; Yeasts
• ISSN: 1469-221X; 1469-3178
• DOI: 10.1038/embor.2013.114

Mitophagy is a process that selectively degrades mitochondria. When mitophagy is induced in yeast, the mitochondrial outer membrane protein Atg32 is phosphorylated, interacts with the adaptor protein Atg11 and is recruited into the vacuole with mitochondria. We screened kinase‐deleted yeast strains and found that CK2 is essential for Atg32 phosphorylation, Atg32–Atg11 interaction and mitophagy. Inhibition of CK2 specifically blocks mitophagy, but not macroautophagy, pexophagy or the Cvt pathway. In vitro , CK2 phosphorylates Atg32 at serine 114 and serine 119. We conclude that CK2 regulates mitophagy by directly phosphorylating Atg32. Atg32 is the yeast mitophagy receptor for mitophagy, a process that selectively degrades mitochondria. Here, CK2 is shown to phosphorylate Atg32 and be essential for Atg32‐Atg11 interaction and ensuing mitophagy.