ArticleMolecular cell2009
Mechanism of substrate unfolding and translocation by the regulatory particle of the proteasome from Methanocaldococcus jannaschii.
Article in Molecular cell, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 55 papers.
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Who cites it
55 citing papers in PubMed, 97 citations in OpenAlex.
- Substrate-interacting pore loops of two ATPase subunits determine the degradation efficiency of the 26S proteasome.Nature communications · 2026Article
- Flotillin-mediated stabilization of unfolded proteins in bacterial membrane microdomains.Nature communications · 2024Article
- Interactome Analysis Identifies MSMEI_3879 as a Substrate of Mycolicibacterium smegmatis ClpC1.Microbiology spectrum · 2023Article
- Assembly chaperone Nas6 selectively destabilizes 26S proteasomes with defective regulatory particle-core particle interfaces.The Journal of biological chemistry · 2023Article
- Simulating the directional translocation of a substrate by the AAA+ motor in the 26S proteasome.Proceedings of the National Academy of Sciences of the United States of America · 2021Article
- Structure, Dynamics and Function of the 26S Proteasome.Sub-cellular biochemistry · 2021Review
- Observing Protein Degradation by the PAN-20S Proteasome by Time-Resolved Neutron Scattering.Biophysical journal · 2020Article
- Stairway to translocation: AAA+ motor structures reveal the mechanisms of ATP-dependent substrate translocation.Protein science : a publication of the Protein Society · 2020Review
- Proteolytic systems of archaea: slicing, dicing, and mincing in the extreme.Emerging topics in life sciences · 2018Article
- Structural mechanism for nucleotide-driven remodeling of the AAA-ATPase unfoldase in the activated human 26S proteasome.Nature communications · 2018Article
- Conformational Landscape of the p28-Bound Human Proteasome Regulatory Particle.Molecular cell · 2017Article
- The Proteasomal ATPases Use a Slow but Highly Processive Strategy to Unfold Proteins.Frontiers in molecular biosciences · 2017Article
- Structural basis for dynamic regulation of the human 26S proteasome.Proceedings of the National Academy of Sciences of the United States of America · 2016Article
- Conserved Sequence Preferences Contribute to Substrate Recognition by the Proteasome.The Journal of biological chemistry · 2016Article
- Article
- Mechanistic and Structural Insights into the Prion-Disaggregase Activity of Hsp104.Journal of molecular biology · 2016Review
- ahg12 is a dominant proteasome mutant that affects multiple regulatory systems for germination of Arabidopsis.Scientific reports · 2016Article
- ATP binding to neighbouring subunits and intersubunit allosteric coupling underlie proteasomal ATPase function.Nature communications · 2015Article
- Structural and biochemical properties of an extreme 'salt-loving' proteasome activating nucleotidase from the archaeon Haloferax volcanii.Extremophiles : life under extreme conditions · 2014Article
- Structure of the Rpn11-Rpn8 dimer reveals mechanisms of substrate deubiquitination during proteasomal degradation.Nature structural & molecular biology · 2014Article
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Authors and funding
6 authors at 3 institutions in 2 countries.
Funding
Abstract
In the archaebacterium Methanocaldococcus jannaschii (M. jannaschii), the proteasomal regulatory particle (RP), a homohexameric complex of proteasome-activating nucleotidase (PAN), is responsible for target protein recognition, followed by unfolding and translocation of the bound protein into the core particle (CP) for degradation. Guided by structure-based mutagenesis, we identify amino acids and structural motifs that are essential for PAN function. Key residues line the axial channel of PAN, defining the apparent pathway of substrate translocation. Subcomplex II of PAN, comprising the ATPase domain, associates with the CP and drives ATP-dependent unfolding of the substrate protein, whereas the distal subcomplex I forms the entry port of the substrate translocation channel. A linker segment between subcomplexes I and II is essential for PAN function, implying functional and perhaps mechanical coupling between these domains. Sequence conservation suggests that the principles of PAN function are likely to apply to the proteasomal RP of eukaryotes.
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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.