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Autophagy 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. Copyright © 2020 The Authors. Published by Elsevier Inc. All rights reserved.


Florian Wilfling, Chia-Wei Lee, Philipp S Erdmann, Yumei Zheng, Dawafuti Sherpa, Stefan Jentsch, Boris Pfander, Brenda A Schulman, Wolfgang Baumeister. A Selective Autophagy Pathway for Phase-Separated Endocytic Protein Deposits. Molecular cell. 2020 Dec 03;80(5):764-778.e7

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PMID: 33207182

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