In Caenorhabditis elegans embryos, paternally provided organelles, including mitochondria, are eliminated by a process of selective autophagy called allophagy, the mechanism by which mitochondrial DNA is inherited maternally. However, it remains unclear how paternal organelles are recognized and targeted for autophagy. Here, we identified an autophagy receptor for allophagy, ALLO-1. ALLO-1 is essential for autophagosome formation around paternal organelles and directly binds to the worm LC3 homologue LGG-1 through its LC3-interacting region (LIR) motif. After fertilization, ALLO-1 accumulates on the paternal organelles before autophagosome formation, and this localization depends on the ubiquitin modification of the paternal organelles. We also identified IKKE-1, a worm homologue of the TBK1 and IKKε family kinase, as another critical regulator of allophagy. IKKE-1 interacts with ALLO-1, and the IKKE-1-dependent phosphorylation of ALLO-1 is important for paternal organelle clearance. Thus, we propose that ALLO-1 is the allophagy receptor whose function is regulated by IKKE-1-dependent phosphorylation.

中文翻译：

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自噬受体ALLO-1和IKKE-1激酶控制秀丽隐杆线虫父本线粒体的清除。

在秀丽隐杆线虫胚胎中，由父体提供的细胞器（包括线粒体）通过称为自噬的选择性自噬过程被消除，该过程是线粒体DNA在母体中遗传的机制。然而，尚不清楚父细胞器如何被识别并靶向自噬。在这里，我们确定了自噬受体的Allo-1。ALLO-1对于父体细胞器周围自噬体形成至关重要，并通过其LC3相互作用区域（LIR）主题直接与蠕虫LC3同源LGG-1结合。受精后，ALLO-1会在自噬小体形成之前积聚在父本细胞器上，而这种定位取决于父本细胞器的泛素修饰。我们还确定了IKKE-1，它是TBK1和IKKε家族激酶的蠕虫同源物，作为同化的另一个重要调节剂。IKKE-1与ALLO-1相互作用，且ALLO-1的IKKE-1依赖性磷酸化对于清除父辈细胞器很重要。因此，我们提出ALLO-1是同种异体受体，其功能受IKKE-1依赖性磷酸化调节。