Proteasome activator Blm10 levels and autophagic degradation directly impact the proteasome landscape
| Autor: | Jeroen Roelofs, Samuel Ockerhausen, Zachary Reuter, Kenrick A. Waite, Alicia Burris |
|---|---|
| Rok vydání: | 2021 |
| Předmět: |
0301 basic medicine
Cytoplasm Proteasome Endopeptidase Complex autophagy Saccharomyces cerevisiae Proteins Endogeny Saccharomyces cerevisiae yeast YPD yeast peptone dextrose Protein degradation Biochemistry 03 medical and health sciences Ubiquitin ubiquitin Molecular Biology proteasome storage granule 030102 biochemistry & molecular biology biology PSG proteasome storage granule Activator (genetics) Chemistry Autophagy stress response Cell Biology CP core particle Phenotype Cell biology proteasome 030104 developmental biology RP regulatory particle Proteasome protein degradation biology.protein Blm10 Protein Processing Post-Translational Function (biology) Research Article |
| Zdroj: | The Journal of Biological Chemistry |
| ISSN: | 0021-9258 |
| DOI: | 10.1016/j.jbc.2021.100468 |
| Popis: | The proteasome selectively degrades proteins. It consists of a core particle (CP), which contains proteolytic active sites that can associate with different regulators to form various complexes. How these different complexes are regulated and affected by changing physiological conditions, however, remains poorly understood. In this study, we focused on the activator Blm10 and the regulatory particle (RP). In yeast, increased expression of Blm10 outcompeted RP for CP binding, which suggests that controlling the cellular levels of Blm10 can affect the relative amounts of RP-bound CP. While strong overexpression of BLM10 almost eliminated the presence of RP-CP complexes, the phenotypes this should induce were not observed. Our results show this was due to the induction of Blm10-CP autophagy under prolonged growth in YPD. Similarly, under conditions of endogenous BLM10 expression, Blm10 was degraded through autophagy as well. This suggests that reducing the levels of Blm10 allows for more CP-binding surfaces and the formation of RP-CP complexes under nutrient stress. This work provides important insights into maintaining the proteasome landscape and how protein expression levels affect proteasome function. |
| Databáze: | OpenAIRE |
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