ArticleProceedings of the National Academy of Sciences of the United States of America2012
Dual functions of the Hsm3 protein in chaperoning and scaffolding regulatory particle subunits during the proteasome assembly.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 45 papers, 1 of them a synthesis that pooled it.
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Who cites it
45 citing papers in PubMed, 1 synthesis or guideline pooled it.
- The proteasome as a druggable target with multiple therapeutic potentialities: Cutting and non-cutting edges.Pharmacology & therapeutics · 2020Pooled it
- 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
- Chaperones shape the conformational landscape of 26S-proteasome-base assembly for allosteric ATPase motor activation.bioRxiv : the preprint server for biology · 2026Article
- Plasticity in the structure and assembly of proteasomes.The Journal of biological chemistry · 2026Review
- More 26S and 30S proteasomes are beneficial in proteinopathy.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Bi-handed assembly chaperones regulate protein complex assembly through an intramolecular handover mechanism.Science advances · 2025Article
- Spatial mechanisms of quality control during chaperone-mediated assembly of the proteasome.Nature communications · 2025Article
- Stepwise order in protein complex assembly: approaches and emerging themes.Open biology · 2025Review
- Phase-separated ribosome-nascent chain complexes in genotoxic stress response.RNA (New York, N.Y.) · 2023Article
- Wiggle and Shake: Managing and Exploiting Conformational Dynamics during Proteasome Biogenesis.Biomolecules · 2023Review
- Assembly checkpoint of the proteasome regulatory particle is activated by coordinated actions of proteasomal ATPase chaperones.Cell reports · 2022Article
- Cooperativity in Proteasome Core Particle Maturation.iScience · 2020Article
- Two alternative mechanisms regulate the onset of chaperone-mediated assembly of the proteasomal ATPases.The Journal of biological chemistry · 2019Article
- Co-translational assembly of proteasome subunits in NOT1-containing assemblysomes.Nature structural & molecular biology · 2019Article
- An Allosteric Interaction Network Promotes Conformation State-Dependent Eviction of the Nas6 Assembly Chaperone from Nascent 26S Proteasomes.Cell reports · 2019Article
- Dynamic Regulation of the 26S Proteasome: From Synthesis to Degradation.Frontiers in molecular biosciences · 2019Review
- Nuclear Transport of Yeast Proteasomes.Frontiers in molecular biosciences · 2019Review
- Ubiquitin-dependent switch during assembly of the proteasomal ATPases mediated by Not4 ubiquitin ligase.Proceedings of the National Academy of Sciences of the United States of America · 2018Article
- Regulation of proteasome assembly and activity in health and disease.Nature reviews. Molecular cell biology · 2018Review
- PSMD5 Inactivation Promotes 26S Proteasome Assembly during Colorectal Tumor Progression.Cancer research · 2018Article
Corrections and comments
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Authors and funding
12 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The 26S proteasome, a molecular machine responsible for regulated protein degradation, consists of a proteolytic core particle (20S CP) associated with 19S regulatory particles (19S RPs) subdivided into base and lid subcomplexes. The assembly of 19S RP base subcomplex is mediated by multiple dedicated chaperones. Among these, Hsm3 is important for normal growth and directly targets the carboxyl-terminal (C-terminal) domain of Rpt1 of the Rpt1-Rpt2-Rpn1 assembly intermediate. Here, we report crystal structures of the yeast Hsm3 chaperone free and bound to the C-terminal domain of Rpt1. Unexpectedly, the structure of the complex suggests that within the Hsm3-Rpt1-Rpt2 module, Hsm3 also contacts Rpt2. We show that in both yeast and mammals, Hsm3 actually directly binds the AAA domain of Rpt2. The Hsm3 C-terminal region involved in this interaction is required in vivo for base assembly, although it is dispensable for binding Rpt1. Although Rpt1 and Rpt2 exhibit weak affinity for each other, Hsm3 unexpectedly acts as an essential matchmaker for the Rpt1-Rpt2-Rpn1 assembly by bridging both Rpt1 and Rpt2. In addition, we provide structural and biochemical evidence on how Hsm3/S5b may regulate the 19S RP association to the 20S CP proteasome. Our data point out the diverse functions of assembly chaperones.
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