Autophagy eliminates cytoplasmic content selected by autophagy receptors, which link cargoes to the membrane bound autophagosomal ubiquitin-like protein Atg8/LC3. Here, we discover a selective autophagy pathway for protein condensates formed by endocytic proteins. In this pathway, the endocytic yeast protein Ede1 functions as a selective autophagy receptor. Distinct domains within Ede1 bind Atg8 and mediate phase separation into condensates. Both properties are necessary for an Ede1-dependent autophagy pathway for endocytic proteins, which differs from regular endocytosis, does not involve other known selective autophagy receptors, but requires the core autophagy machinery. Cryo-electron tomography of Ede1-containing condensates - at the plasma membrane and in autophagic bodies - shows a phase-separated compartment at the beginning and end of the Ede1-mediated selective autophagy pathway. Our data suggest a model for autophagic degradation of membraneless compartments by the action of intrinsic autophagy receptors.

中文翻译：

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选择性自噬途径用于相分离的内吞性蛋白质沉积

自噬消除了自噬受体选择的细胞质含量，自噬受体将货物与膜结合的自噬泛素样蛋白Atg8 / LC3连接起来。在这里，我们发现内吞性蛋白质形成的蛋白质凝结物的选择性自噬途径。在该途径中，内吞酵母蛋白Ede1用作选择性自噬受体。Ede1中的不同域与Atg8结合并介导相分离成冷凝物。这两种特性对于依赖Ede1的内吞蛋白自噬途径都是必需的，这不同于常规的内吞作用，不涉及其他已知的选择性自噬受体，但需要核心自噬机制。在质膜和自噬体中，含Ede1的冷凝物的低温电子断层扫描显示在Ede1介导的选择性自噬途径的开始和结束时相分离的隔室。我们的数据提出了一种通过固有自噬受体的作用自噬降解无膜隔室的模型。