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Full-Text Articles in Biochemistry
Autophagic Turnover Of Inactive 26s Proteasomes In Yeast Is Directed By The Ubiquitin Receptor Cue5 And The Hsp42 Chaperone, Richard S. Marshall, Fionn Mcloughlin, Richard D. Vierstra
Autophagic Turnover Of Inactive 26s Proteasomes In Yeast Is Directed By The Ubiquitin Receptor Cue5 And The Hsp42 Chaperone, Richard S. Marshall, Fionn Mcloughlin, Richard D. Vierstra
Biology Faculty Publications & Presentations
Highlights
- The yeast 26S proteasome is degraded by Atg8-mediated autophagy
- Nitrogen starvation and inactivation stimulate proteaphagy via distinct pathways
- Proteasome inhibition is accompanied by extensive ubiquitylation of the complex
- Proteaphagy engages the Cue5 autophagy receptor and the Hsp42 chaperone
Summary
The autophagic clearance of 26S proteasomes (proteaphagy) is an important homeostatic mechanism within the ubiquitin system that modulates proteolytic capacity and eliminates damaged particles. Here, we define two proteaphagy routes in yeast that respond to either nitrogen starvation or particle inactivation. Whereas the core autophagic machineries required for Atg8 lipidation and vesiculation are essential for both routes, the upstream Atg1 …