Atg43 tethers isolation membranes to mitochondria to promote starvation-induced mitophagy in fission yeast.
Atg43 tethers isolation membranes to mitochondria to promote starvation-induced mitophagy in fission yeast.
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DOI：
10.7554/elife.61245
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发表时间：
2020-11-03
期刊：
影响因子：
7.7
通讯作者：
Kanki T
中科院分区：
文献类型：
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作者：
Fukuda T;Ebi Y;Saigusa T;Furukawa K;Yamashita SI;Inoue K;Kobayashi D;Yoshida Y;Kanki T
通过线粒体自噬的线粒体降解有助于维持线粒体功能。在这项研究中，我们确定，Atg 43，线粒体外膜蛋白，作为一个线粒体自噬受体的模式生物裂殖酵母粟酒裂殖酵母，以促进线粒体的选择性降解。Atg 43含有线粒体自噬所必需的Atg 8家族相互作用基序。Atg 8的强制招聘线粒体恢复线粒体自噬Atg 43缺陷的细胞，表明Atg 43系扩大隔离膜线粒体。我们发现，线粒体输入因子，包括Mim 1-Mim 2复合物和Tom 70，是至关重要的线粒体自噬。Atg 43的人工线粒体负载绕过了输入因子的要求，表明它们通过Atg 43促进线粒体自噬。Atg 43不仅在饥饿期间维持生长能力，而且通过其不依赖于线粒体的功能促进营养生长。Atg 43是研究真核生物线粒体自噬的机制、生理作用以及起源和进化的一个有用的模型。
Degradation of mitochondria through mitophagy contributes to the maintenance of mitochondrial function. In this study, we identified that Atg43, a mitochondrial outer membrane protein, serves as a mitophagy receptor in the model organism Schizosaccharomyces pombe to promote the selective degradation of mitochondria. Atg43 contains an Atg8-family-interacting motif essential for mitophagy. Forced recruitment of Atg8 to mitochondria restores mitophagy in Atg43-deficient cells, suggesting that Atg43 tethers expanding isolation membranes to mitochondria. We found that the mitochondrial import factors, including the Mim1–Mim2 complex and Tom70, are crucial for mitophagy. Artificial mitochondrial loading of Atg43 bypasses the requirement of the import factors, suggesting that they contribute to mitophagy through Atg43. Atg43 not only maintains growth ability during starvation but also facilitates vegetative growth through its mitophagy-independent function. Thus, Atg43 is a useful model to study the mechanism and physiological roles, as well as the origin and evolution, of mitophagy in eukaryotes.