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A Selective Autophagy Pathway for Phase-Separated Endocytic Protein Deposits
Florian Wilfling1, Chia-Wei Lee2, Philipp S Erdmann3
1Molecular Cell Biology, Max Planck Institute of Biochemistry, 82152 Martinsried, Germany; Molecular Structural Biology, Max Planck Institute of Biochemistry, 82152 Martinsried, Germany; Molecular Machines and Signaling, Max Planck Institute of Biochemistry, 82152 Martinsried, Germany.
Molecular Cell
|November 18, 2020
Summary
Researchers discovered a new selective autophagy pathway in yeast that degrades protein condensates using the endocytic protein Ede1 as a specific receptor, distinct from known pathways.
Area of Science:
- Cell Biology
- Molecular Biology
- Yeast Genetics
Background:
- Autophagy degrades cellular components via selective autophagy receptors linking cargo to Atg8/LC3.
- Understanding selective autophagy pathways is crucial for cellular quality control.
Purpose of the Study:
- To investigate a novel selective autophagy pathway for protein condensates in yeast.
- To identify the role of the endocytic protein Ede1 in this pathway.
Main Methods:
- Utilized yeast genetics and cryo-electron tomography.
- Investigated the binding domains of Ede1 to Atg8 and its role in phase separation.
- Analyzed the Ede1-dependent autophagy pathway for endocytic proteins.
Main Results:
- Identified Ede1 as a selective autophagy receptor for endocytic protein condensates.
- Demonstrated that Ede1 binds Atg8 and mediates phase separation, essential for the pathway.
- Showcased a distinct autophagy route requiring core machinery but not other known receptors.
- Cryo-electron tomography visualized Ede1 condensates in a phase-separated state.
Conclusions:
- Ede1 acts as an intrinsic autophagy receptor for protein condensates.
- This pathway represents a novel mechanism for degrading macromolecular protein complexes via selective autophagy.
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