ArticleNature communications2024
Structural basis of human 20S proteasome biogenesis.
Article in Nature communications, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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Who cites it
13 citing papers in PubMed.
- Molecular architecture and spatial organization of proteasomes in the human sperm nucleus.Nature structural & molecular biology · 2026Article
- Integrative analysis identifies candidate biomarkers for bladder cancer: evidence from genomic and clinical validation.Molecular biology reports · 2026Article
- Dominant-negative PSMB10 disrupts immunoproteasome assembly and leads to transient T lymphopenia.Journal of human immunity · 2026Article
- Magical moments in protease biology: proteasome autocatalytic activation and PI31-mediated inhibition.Trends in biochemical sciences · 2026Review
- Structural transitions in the stepwise assembly of proteasome core particles.Nature communications · 2026Article
- Molecular mechanisms in rare proteasomopathies.EULAR rheumatology open · 2026Review
- TOGR3, a Proteasome β4 Subunit, Orchestrates Sugar Homeostasis to Trade Off Growth and Thermotolerance in Rice.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026Article
- Engineering TCR-directed T-cells for the treatment of multiple myeloma.Frontiers in immunology · 2026Review
- Proteasome Assembly Chaperone 3 Defines Metabolic-Immune Programs and Poor Prognosis in Breast Cancer via Multi-Omics Approaches.Journal of Cancer · 2026Article
- A recombinant expression system for thebioRxiv : the preprint server for biology · 2025Article
- PI31 is a positive regulator of 20S immunoproteasome assembly.Journal of cell science · 2025Article
- Structural basis for allosteric modulation of M. tuberculosis proteasome core particle.Nature communications · 2025Article
- Stepwise order in protein complex assembly: approaches and emerging themes.Open biology · 2025Review
Corrections and comments
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Authors and funding
4 authors.
Funding
Abstract
New proteasomes are produced to accommodate increases in cellular catabolic demand and prevent the accumulation of cytotoxic proteins. Formation of the proteasomal 20S core complex relies on the function of the five chaperones PAC1-4 and POMP. Here, to understand how these chaperones facilitate proteasome assembly, we tagged the endogenous chaperones using CRISPR/Cas gene editing and examined the chaperone-bound complexes by cryo-EM. We observe an early α-ring intermediate subcomplex that is stabilized by PAC1-4, which transitions to β-ring assembly upon dissociation of PAC3/PAC4 and rearrangement of the PAC1 N-terminal tail. Completion of the β-ring and dimerization of half-proteasomes repositions critical lysine K33 to trigger cleavage of the β pro-peptides, leading to the concerted dissociation of POMP and PAC1/PAC2 to yield mature 20S proteasomes. This study reveals structural insights into critical points along the assembly pathway of the human proteasome and provides a molecular blueprint for 20S biogenesis.
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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.