ArticleScientific reports2016
Phosphorylation of the C-terminal tail of proteasome subunit α7 is required for binding of the proteasome quality control factor Ecm29.
Article in Scientific reports, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.
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Who cites it
20 citing papers in PubMed, 28 citations in OpenAlex.
- Regulation via compartmentation: adaptive localization of the proteasome under stress.Biochemical Society transactions · 2025Review
- AMPK alters proteasome phosphorylation status and prevents persistent proteasome condensates.Genetics · 2025Article
- Mechanisms and regulation of substrate degradation by the 26S proteasome.Nature reviews. Molecular cell biology · 2025Review
- Method of Monitoring 26S Proteasome in Cells Revealed the Crucial Role of PSMA3 C-Terminus in 26S Integrity.Biomolecules · 2023Article
- Article
- Assembly chaperone Nas6 selectively destabilizes 26S proteasomes with defective regulatory particle-core particle interfaces.The Journal of biological chemistry · 2023Article
- Structure of the reduced microsporidian proteasome bound by PI31-like peptides in dormant spores.Nature communications · 2022Article
- Oxidative and salt stresses alter the 26S proteasome holoenzyme and associated protein profiles in Arabidopsis thaliana.BMC plant biology · 2021Article
- Expanding the role of proteasome homeostasis in Parkinson's disease: beyond protein breakdown.Cell death & disease · 2021Review
- Structure, Dynamics and Function of the 26S Proteasome.Sub-cellular biochemistry · 2021Review
- Proteasome Biology: Chemistry and Bioengineering Insights.Polymers · 2020Review
- Ecm29-mediated proteasomal distribution modulates excitatory GABA responses in the developing brain.The Journal of cell biology · 2020Article
- Phosphorylation Modifications Regulating Cardiac Protein Quality Control Mechanisms.Frontiers in physiology · 2020Review
- Dynamic Regulation of the 26S Proteasome: From Synthesis to Degradation.Frontiers in molecular biosciences · 2019Review
- Regulation of Proteasome Activity by (Post-)transcriptional Mechanisms.Frontiers in molecular biosciences · 2019Review
- Adaptive homeostasis and the free radical theory of ageing.Free radical biology & medicine · 2018Review
- Autophagic clearance of proteasomes in yeast requires the conserved sorting nexin Snx4.The Journal of biological chemistry · 2017Article
- Regulating protein breakdown through proteasome phosphorylation.The Biochemical journal · 2017Review
- Reversible phosphorylation of the 26S proteasome.Protein & cell · 2017Review
- Proteasome activator Blm10 levels and autophagic degradation directly impact the proteasome landscape.The Journal of biological chemistryArticle
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
Abstract
The proteasome degrades many short-lived proteins that are labeled with an ubiquitin chain. The identification of phosphorylation sites on the proteasome subunits suggests that degradation of these substrates can also be regulated at the proteasome. In yeast and humans, the unstructured C-terminal region of α7 contains an acidic patch with serine residues that are phosphorylated. Although these were identified more than a decade ago, the molecular implications of α7 phosphorylation have remained unknown. Here, we showed that yeast Ecm29, a protein involved in proteasome quality control, requires the phosphorylated tail of α7 for its association with proteasomes. This is the first example of proteasome phosphorylation dependent binding of a proteasome regulatory factor. Ecm29 is known to inhibit proteasomes and is often found enriched on mutant proteasomes. We showed that the ability of Ecm29 to bind to mutant proteasomes requires the α7 tail binding site, besides a previously characterized Rpt5 binding site. The need for these two binding sites, which are on different proteasome subcomplexes, explains the specificity of Ecm29 for proteasome holoenzymes. We propose that alterations in the relative position of these two sites in different conformations of the proteasome provides Ecm29 the ability to preferentially bind specific proteasome conformations.
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