ArticleThe Journal of biological chemistry2012
Structure of a proteasome Pba1-Pba2 complex: implications for proteasome assembly, activation, and biological function.
Article in The Journal of biological chemistry, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 40 papers.
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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.
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Who cites it
40 citing papers in PubMed, 63 citations in OpenAlex.
- Structural transitions in the stepwise assembly of proteasome core particles.Nature communications · 2026Article
- The α5-α6-α7-Pba3-Pba4 Complex: A Starting Unit in Proteasome Core Particle Assembly.Biomolecules · 2025Article
- Structural roles of Ump1 and β-subunit propeptides in proteasome biogenesis.Life science alliance · 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
- 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
- Rapid, scalable, combinatorial genome engineering by marker-less enrichment and recombination of genetically engineered loci in yeast.Cell reports methods · 2023Article
- PKR Protects the Major Catalytic Subunit of PKA Cpk1 from FgBlm10-Mediated Proteasome Degradation inInternational journal of molecular sciences · 2022Article
- Review
- Mechanism of proteasome gate modulation by assembly chaperones Pba1 and Pba2.The Journal of biological chemistry · 2022Article
- Chaperone-mediated assembly of the proteasome core particle - recent developments and structural insights.Journal of cell science · 2022Review
- The YΦ motif defines the structure-activity relationships of human 20S proteasome activators.Nature communications · 2022Article
- Proteasome Control of [URE3] Prion Propagation by Degradation of Anti-Prion Proteins Cur1 and Btn2 in Saccharomyces cerevisiae.Genetics · 2021Article
- How to build a proteasome.Nature structural & molecular biology · 2021Article
- Structure, Dynamics and Function of the 26S Proteasome.Sub-cellular biochemistry · 2021Review
- An evolutionarily distinct chaperone promotes 20S proteasome α-ring assembly in plants.Journal of cell science · 2020Article
- Supramolecular tholos-like architecture constituted by archaeal proteins without functional annotation.Scientific reports · 2020Article
- Proteomic analysis of affinity-purified 26S proteasomes identifies a suite of assembly chaperones inThe Journal of biological chemistry · 2019Article
Corrections and comments
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Authors and funding
9 authors at 2 institutions in 1 country.
Funding
Abstract
The 20S proteasome is an essential, 28-subunit protease that sequesters proteolytic sites within a central chamber, thereby repressing substrate degradation until proteasome activators open the entrance/exit gate. Two established activators, Blm10 and PAN/19S, induce gate opening by binding to the pockets between proteasome α-subunits using C-terminal HbYX (hydrophobic-tyrosine-any residue) motifs. Equivalent HbYX motifs have been identified in Pba1 and Pba2, which function in proteasome assembly. Here, we demonstrate that Pba1-Pba2 proteins form a stable heterodimer that utilizes its HbYX motifs to bind mature 20S proteasomes in vitro and that the Pba1-Pba2 HbYX motifs are important for a physiological function of proteasomes, the maintenance of mitochondrial function. Other factors that contribute to proteasome assembly or function also act in the maintenance of mitochondrial function and display complex genetic interactions with one another, possibly revealing an unexpected pathway of mitochondrial regulation involving the Pba1-Pba2 proteasome interaction. Our determination of a proteasome Pba1-Pba2 crystal structure reveals a Pba1 HbYX interaction that is superimposable with those of known activators, a Pba2 HbYX interaction that is different from those reported previously, and a gate structure that is disrupted but not sufficiently open to allow entry of even small peptides. These findings extend understanding of proteasome interactions with HbYX motifs and suggest multiple roles for Pba1-Pba2 interactions throughout proteasome assembly and function.
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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.