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6wy6
From Proteopedia
Crystal structure of S. cerevisiae Atg8 in complex with Ede1 (1220-1247)
Structural highlights
FunctionATG8_YEAST Involved in cytoplasm to vacuole transport (Cvt) vesicles and autophagosomes formation. With ATG4, may mediate the delivery of the vesicles and autophagosomes to the vacuole via the microtubule cytoskeleton. Participates also in membrane fusion events that take place in the early secretory pathway.[1] [2] [3] [4] [5] [6] [7] [8] [9] Publication Abstract from PubMedAutophagy 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. A Selective Autophagy Pathway for Phase-Separated Endocytic Protein Deposits.,Wilfling F, Lee CW, Erdmann PS, Zheng Y, Sherpa D, Jentsch S, Pfander B, Schulman BA, Baumeister W Mol Cell. 2020 Dec 3;80(5):764-778.e7. doi: 10.1016/j.molcel.2020.10.030. Epub , 2020 Nov 17. PMID:33207182[10] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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