ArticleThe Biochemical journal2009
Variably modulated gating of the 26S proteasome by ATP and polyubiquitin.
Article in The Biochemical journal, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 33 papers.
What it found
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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.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
33 citing papers in PubMed, 54 citations in OpenAlex.
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- Targeting Proteasomes and the MHC Class I Antigen Presentation Machinery to Treat Cancer, Infections and Age-Related Diseases.Cancers · 2023Review
- High resolution structures define divergent and convergent mechanisms of archaeal proteasome activation.Communications biology · 2023Article
- Proteasome substrate receptors and their therapeutic potential.Trends in biochemical sciences · 2022Review
- Allostery Modulates Interactions between Proteasome Core Particles and Regulatory Particles.Biomolecules · 2022Review
- Proteasome interaction with ubiquitinated substrates: from mechanisms to therapies.The FEBS journal · 2021Review
- Structure, Dynamics and Function of the 26S Proteasome.Sub-cellular biochemistry · 2021Review
- Degradation of Intrinsically Disordered Proteins by the NADH 26S Proteasome.Biomolecules · 2020Article
- Proteins containing ubiquitin-like (Ubl) domains not only bind to 26S proteasomes but also induce their activation.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- Ubiquitin receptors are required for substrate-mediated activation of the proteasome's unfolding ability.Scientific reports · 2019Article
- ZFAND5/ZNF216 is an activator of the 26S proteasome that stimulates overall protein degradation.Proceedings of the National Academy of Sciences of the United States of America · 2018Article
- Structure and Function of the 26S Proteasome.Annual review of biochemistry · 2018Review
- The deubiquitinating enzyme Usp14 allosterically inhibits multiple proteasomal activities and ubiquitin-independent proteolysis.The Journal of biological chemistry · 2017Article
- Substrate Ubiquitination Controls the Unfolding Ability of the Proteasome.The Journal of biological chemistry · 2016Article
- The life cycle of the 26S proteasome: from birth, through regulation and function, and onto its death.Cell research · 2016Review
- Open-gate mutants of the mammalian proteasome show enhanced ubiquitin-conjugate degradation.Nature communications · 2016Article
- Protein Folding and Mechanisms of Proteostasis.International journal of molecular sciences · 2015Review
- Paradigms of protein degradation by the proteasome.Current opinion in structural biology · 2014Review
- Regulated protein turnover: snapshots of the proteasome in action.Nature reviews. Molecular cell biology · 2014Review
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
The 26S proteasome is a 2500 kDa protease complex that degrades polyubiquitylated proteins by a mechanism that requires ATP hydrolysis. It also degrades short non-ubiquitylated peptides and certain unstructured proteins by an energy-independent mechanism that requires bound ATP to maintain its component subcomplexes, the 20S proteasome and PA700, in a functionally assembled state. Proteolysis of both types of substrate requires PA700-induced opening of reversible gates at substrate-access pores of the 20S proteasome. In the present study we demonstrate that the rate of peptide substrate hydrolysis, a functional monitor of gate opening, is regulated variably by multiple effectors. ATPgammaS (adenosine 5'-[gamma-thio]triphosphate) and other non-hydrolysable ATP analogues increased peptide substrate hydrolysis by intact 26S proteasomes. Thus nucleotides that maintained 26S proteasome structure, but did not support ATP hydrolysis or the degradation of polyubiquitylated proteins, promoted enhanced rates of peptide hydrolysis. Polyubiquitin and a peptoid that binds selectively to a single ATPase subunit of PA700 also increased rates of peptide hydrolysis but had disparate effects on rates of ATP hydrolysis. The effect of polyubiquitin was specific for ubiquitin-ubiquitin linkages that supported proteolysis of protein substrates. These results indicate that gating of the 26S proteasome is not a simple two-state process but can be variably modulated. Our results suggest that modulated gating of the proteasome may be an important element of the mechanism of proteolysis of polyubiquitylated proteins.
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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.