Laboratory of Biosignaling, Niigata University Graduate School of Medical and Dental Sciences, Niigata 951-8510.
EMBO Rep. 2013 Sep;14(9):788-94. doi: 10.1038/embor.2013.114. Epub 2013 Jul 30.
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.
自噬是一种选择性降解线粒体的过程。在酵母中诱导自噬时，线粒体膜外蛋白 Atg32 被磷酸化，与衔接蛋白 Atg11 相互作用，并与线粒体一起被募集到液泡中。我们筛选了激酶缺失的酵母菌株，发现 CK2 对 Atg32 的磷酸化、Atg32-Atg11 相互作用和自噬是必需的。CK2 的抑制特异性地阻断自噬，但不阻断巨自噬、pexophagy 或 Cvt 途径。在体外，CK2 磷酸化 Atg32 的丝氨酸 114 和丝氨酸 119。我们得出结论，CK2 通过直接磷酸化 Atg32 来调节自噬。
