ArticleScientific reports2019
Proteasome subunit α1 overexpression preferentially drives canonical proteasome biogenesis and enhances stress tolerance in yeast.
Article in Scientific reports, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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Who cites it
14 citing papers in PubMed, 18 citations in OpenAlex.
- Mapping Interaction of Assembly Factor Rpn14 With the Proteasome Base Reveals a Bipartite Interface and Implies Ordered Remodeling of Intersubunit Contacts During Proteasome Biogenesis.Journal of molecular biology · 2026Article
- Plasticity in the structure and assembly of proteasomes.The Journal of biological chemistry · 2026Review
- Hyperactive 20Science advances · 2025Article
- Wiggle and Shake: Managing and Exploiting Conformational Dynamics during Proteasome Biogenesis.Biomolecules · 2023Review
- Substrate-specific effects of natural genetic variation on proteasome activity.PLoS genetics · 2023Article
- Chaperone-mediated assembly of the proteasome core particle - recent developments and structural insights.Journal of cell science · 2022Review
- Article
- miR-1 sustains muscle physiology by controlling V-ATPase complex assembly.Science advances · 2021Article
- Research progress on proteasome subunits in regulating occurrence and development of hepatocellular carcinoma.Zhejiang da xue xue bao. Yi xue ban = Journal of Zhejiang University. Medical sciences · 2021Review
- Wake-sleep cycles are severely disrupted by diseases affecting cytoplasmic homeostasis.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- An evolutionarily distinct chaperone promotes 20S proteasome α-ring assembly in plants.Journal of cell science · 2020Article
- Concise Chemoenzymatic Total Synthesis and Identification of Cellular Targets of Cepafungin I.Cell chemical biology · 2020Article
- ER-Resident Transcription Factor Nrf1 Regulates Proteasome Expression and Beyond.International journal of molecular sciences · 2020Review
- A suite of polymerase chain reaction-based peptide tagging plasmids for epitope-targeted enzymatic functionalization of yeast proteins.Yeast (Chichester, England) · 2020Article
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
The 26S proteasome conducts the majority of regulated protein catabolism in eukaryotes. At the heart of the proteasome is the barrel-shaped 20S core particle (CP), which contains two β-rings sandwiched between two α-rings. Whereas canonical CPs contain α-rings with seven subunits arranged α1-α7, a non-canonical CP in which a second copy of the α4 subunit replaces the α3 subunit occurs in both yeast and humans. The mechanisms that control canonical versus non-canonical CP biogenesis remain poorly understood. Here, we have repurposed a split-protein reporter to identify genes that can enhance canonical proteasome assembly in mutant yeast producing non-canonical α4-α4 CPs. We identified the proteasome subunit α1 as an enhancer of α3 incorporation, and find that elevating α1 protein levels preferentially drives canonical CP assembly under conditions that normally favor α4-α4 CP formation. Further, we demonstrate that α1 is stoichiometrically limiting for α-ring assembly, and that enhancing α1 levels is sufficient to increase proteasome abundance and enhance stress tolerance in yeast. Together, our data indicate that the abundance of α1 exerts multiple impacts on proteasome assembly and composition, and we propose that the limited α1 levels observed in yeast may prime cells for alternative proteasome assembly following environmental stimuli.
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