Florian WilflingCHIA-WEI LEEPhilipp S. ErdmannYumei ZhengDawafuti SherpaStefan JentschBoris PfanderBrenda A. SchulmanWolfgang Baumeister2023-07-242023-07-242020-1210972765https://scholars.lib.ntu.edu.tw/handle/123456789/634073Autophagy eliminates cytoplasmic content selected by autophagy receptors, which link cargo to the membrane-bound autophagosomal ubiquitin-like protein Atg8/LC3. Here, we report a selective autophagy pathway for protein condensates formed by endocytic proteins in yeast. In this pathway, the endocytic 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 and 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 route. Our data suggest a model for autophagic degradation of macromolecular protein complexes by the action of intrinsic autophagy receptors.enAtg11; Atg8; Ede1; clathrin-mediated endocytosis; intrinsic autophagy receptor; liquid-liquid phase separation; selective autophagyjournal article10.1016/j.molcel.2020.10.030332071822-s2.0-85096619219https://doi.org/10.1016/j.molcel.2020.10.03083610383