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6WY6

Crystal structure of S. cerevisiae Atg8 in complex with Ede1 (1220-1247)

Summary for 6WY6
Entry DOI10.2210/pdb6wy6/pdb
DescriptorAutophagy-related protein 8, EH domain-containing and endocytosis protein 1 (3 entities in total)
Functional Keywordsselective autophagy, clathrin-mediated endocytosis, intrinsic receptor, atg8, ede1, cryo-electron tomography, liquid-liquid phase separation, llps, protein transport
Biological sourceSaccharomyces cerevisiae (Baker's yeast)
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Total number of polymer chains4
Total formula weight33551.89
Authors
Zheng, Y.,Wilfling, F.,Baumeister, W.,Schulman, B.A. (deposition date: 2020-05-12, release date: 2020-12-02, Last modification date: 2023-10-18)
Primary citationWilfling, F.,Lee, C.W.,Erdmann, P.S.,Zheng, Y.,Sherpa, D.,Jentsch, S.,Pfander, B.,Schulman, B.A.,Baumeister, W.
A Selective Autophagy Pathway for Phase-Separated Endocytic Protein Deposits.
Mol.Cell, 80:764-, 2020
Cited by
PubMed Abstract: 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.
PubMed: 33207182
DOI: 10.1016/j.molcel.2020.10.030
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.773 Å)
Structure validation

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건을2024-10-30부터공개중

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