ArticleThe EMBO journal2007
beta-Subunit appendages promote 20S proteasome assembly by overcoming an Ump1-dependent checkpoint.
Article in The EMBO journal, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 87 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
87 citing papers in PubMed.
- Structure of Blm10:13S proteasome intermediate reveals parallel assembly pathways for the proteasome core particle.Nature communications · 2026Article
- Plasticity in the structure and assembly of proteasomes.The Journal of biological chemistry · 2026Review
- Structural transitions in the stepwise assembly of proteasome core particles.Nature communications · 2026Article
- A recombinant expression system for thebioRxiv : the preprint server for biology · 2025Article
- The α5-α6-α7-Pba3-Pba4 Complex: A Starting Unit in Proteasome Core Particle Assembly.Biomolecules · 2025Article
- Spatial mechanisms of quality control during chaperone-mediated assembly of the proteasome.Nature communications · 2025Article
- Molecular basis for the stepwise and faithful maturation of the 20Science advances · 2025Article
- PSMG2 role in tumorigenesis and stemness mediated by protein accumulation, reticulum stress and autophagy.International journal of biological sciences · 2025Article
- Limiting 20S proteasome assembly leads to unbalanced nucleo-cytoplasmic distribution of 26S/30S proteasomes and chronic proteotoxicity.iScience · 2024Article
- Structural roles of Ump1 and β-subunit propeptides in proteasome biogenesis.Life science alliance · 2024Article
- The Structural Role of RPN10 in the 26S Proteasome and an RPN2-Binding Residue on RPN13 Are Functionally Important in Arabidopsis.International journal of molecular sciences · 2024Article
- Structural basis of human 20S proteasome biogenesis.Nature communications · 2024Article
- Visualizing chaperone-mediated multistep assembly of the human 20S proteasome.Nature structural & molecular biology · 2024Article
- Ksp1 is an autophagic receptor protein for the Snx4-assisted autophagy of Ssn2/Med13.Autophagy · 2024Article
- Visualizing chaperone-mediated multistep assembly of the human 20S proteasome.bioRxiv : the preprint server for biology · 2024Article
- Structure of the preholoproteasome reveals late steps in proteasome core particle biogenesis.Nature structural & molecular biology · 2023Article
- Wiggle and Shake: Managing and Exploiting Conformational Dynamics during Proteasome Biogenesis.Biomolecules · 2023Review
- The Ubiquitin-26S Proteasome Pathway and Its Role in the Ripening of Fleshy Fruits.International journal of molecular sciences · 2023Review
- Hsp70 and Hsp110 Chaperones Promote Early Steps of Proteasome Assembly.Biomolecules · 2022Article
- Review
27 more citing papers are in PubMed but not listed here.
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
5 authors.
Funding
Abstract
Proteasomes are responsible for most intracellular protein degradation in eukaryotes. The 20S proteasome comprises a dyad-symmetric stack of four heptameric rings made from 14 distinct subunits. How it assembles is not understood. Most subunits in the central pair of beta-subunit rings are synthesized in precursor form. Normally, the beta5 (Doa3) propeptide is essential for yeast proteasome biogenesis, but overproduction of beta7 (Pre4) bypasses this requirement. Bypass depends on a unique beta7 extension, which contacts the opposing beta ring. The resulting proteasomes appear normal but assemble inefficiently, facilitating identification of assembly intermediates. Assembly occurs stepwise into precursor dimers, and intermediates contain the Ump1 assembly factor and a novel complex, Pba1-Pba2. beta7 incorporation occurs late and is closely linked to the association of two half-proteasomes. We propose that dimerization is normally driven by the beta5 propeptide, an intramolecular chaperone, but beta7 addition overcomes an Ump1-dependent assembly checkpoint and stabilizes the precursor dimer.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.