ArticleNature communications2015
ATP binding to neighbouring subunits and intersubunit allosteric coupling underlie proteasomal ATPase function.
Article in Nature communications, 2015. 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, 57 citations in OpenAlex.
- 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
- Ubiquitin receptor-mediated, ubiquitin-independent targeted protein degradation via 26Science advances · 2026Article
- Molecular mechanisms of mitochondrial AAA+ proteases.The Journal of biological chemistry · 2026Review
- The Bacteriophage VMY 22 Has Enhanced the Stability of Its Functional Proteins via Adaptive Evolution in a Temperature-Varying Environment.Bioengineering (Basel, Switzerland) · 2026Article
- Allosteric regulation of proteolytic machines unveiled by the synergy between cryo-EM and solution NMR spectroscopy.The Biochemical journal · 2025Review
- RNF213 Acts as a Molecular Switch for Cav-1 Ubiquitination and Phosphorylation in Human Cells.Cells · 2025Article
- Complex structure and activation mechanism of arginine kinase McsB by McsA.Nature chemical biology · 2025Article
- Assembly chaperone Nas6 selectively destabilizes 26S proteasomes with defective regulatory particle-core particle interfaces.The Journal of biological chemistry · 2023Article
- Characterization of a small tRNA-binding protein that interacts with the archaeal proteasome complex.Molecular microbiology · 2022Article
- AAA+ proteins: one motor, multiple ways to work.Biochemical Society transactions · 2022Review
- An empirical energy landscape reveals mechanism of proteasome in polypeptide translocation.eLife · 2022Article
- Structure, Dynamics and Function of the 26S Proteasome.Sub-cellular biochemistry · 2021Review
- Stoichiometry of Nucleotide Binding to Proteasome AAA+ ATPase Hexamer Established by Native Mass Spectrometry.Molecular & cellular proteomics : MCP · 2020Article
- Observing Protein Degradation by the PAN-20S Proteasome by Time-Resolved Neutron Scattering.Biophysical journal · 2020Article
- Structural basis for distinct operational modes and protease activation in AAA+ protease Lon.Science advances · 2020Article
- AAA+ ATPases in Protein Degradation: Structures, Functions and Mechanisms.Biomolecules · 2020Review
- The Non-dominant AAA+ Ring in the ClpAP Protease Functions as an Anti-stalling Motor to Accelerate Protein Unfolding and Translocation.Cell reports · 2020Article
- Activation of the unfolded protein response in high glucose treated endothelial cells is mediated by methylglyoxal.Scientific reports · 2019Article
- An Allosteric Interaction Network Promotes Conformation State-Dependent Eviction of the Nas6 Assembly Chaperone from Nascent 26S Proteasomes.Cell reports · 2019Article
- Cryo-EM structures of the archaeal PAN-proteasome reveal an around-the-ring ATPase cycle.Proceedings of the National Academy of Sciences of the United States of America · 2019Article
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
The primary functions of the proteasome are driven by a highly allosteric ATPase complex. ATP binding to only two subunits in this hexameric complex triggers substrate binding, ATPase-20S association and 20S gate opening. However, it is unclear how ATP binding and hydrolysis spatially and temporally coordinates these allosteric effects to drive substrate translocation into the 20S. Here, we use FRET to show that the proteasomal ATPases from eukaryotes (RPTs) and archaea (PAN) bind ATP with high affinity at neighbouring subunits, which complements the well-established spiral-staircase topology of the 26S ATPases. We further show that two conserved arginine fingers in PAN located at the subunit interface work together as a single allosteric unit to mediate the allosteric effects of ATP binding, without altering the nucleotide-binding pattern. Rapid kinetics analysis also shows that ring resetting of a sequential hydrolysis mechanism can be explained by thermodynamic equilibrium binding of ATP. These data support a model whereby these two functionally distinct allosteric networks cooperate to translocate polypeptides into the 20S for degradation.
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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.