ArticleThe Journal of biological chemistry2011
Dependence of proteasome processing rate on substrate unfolding.
Article in The Journal of biological chemistry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 papers.
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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
30 citing papers in PubMed, 46 citations in OpenAlex.
- The known unknowns of the Hsp90 chaperone.eLife · 2024Review
- Protein degradation kinetics measured by microinjection and live-cell fluorescence microscopy.Scientific reports · 2024Article
- Substrate-specific effects of natural genetic variation on proteasome activity.PLoS genetics · 2023Article
- Single molecule microscopy reveals diverse actions of substrate sequences that impair ClpX AAA+ ATPase function.The Journal of biological chemistry · 2022Article
- Review
- Degradation of Intrinsically Disordered Proteins by the NADH 26S Proteasome.Biomolecules · 2020Article
- Mode of targeting to the proteasome determines GFP fate.The Journal of biological chemistry · 2020Article
- Efficiency of the four proteasome subtypes to degrade ubiquitinated or oxidized proteins.Scientific reports · 2020Article
- Impact of Losing hRpn13 Pru or UCHL5 on Proteasome Clearance of Ubiquitinated Proteins and RA190 Cytotoxicity.Molecular and cellular biology · 2020Article
- A Practical Review of Proteasome Pharmacology.Pharmacological reviews · 2019Review
- Substrate-engaged 26Science (New York, N.Y.) · 2018Article
- Proteostasis, oxidative stress and aging.Redox biology · 2017Review
- Capzimin is a potent and specific inhibitor of proteasome isopeptidase Rpn11.Nature chemical biology · 2017Article
- Substrate Ubiquitination Controls the Unfolding Ability of the Proteasome.The Journal of biological chemistry · 2016Article
- Photo-sensitive degron variants for tuning protein stability by light.BMC systems biology · 2014Article
- Intrinsically disordered segments affect protein half-life in the cell and during evolution.Cell reports · 2014Article
- Disordered proteinaceous machines.Chemical reviews · 2014Review
- Ubiquitin-independent proteasomal degradation.Biochimica et biophysica acta · 2014Review
- The proteasome-associated protein Ecm29 inhibits proteasomal ATPase activity and in vivo protein degradation by the proteasome.The Journal of biological chemistry · 2013Article
- The ATP costs and time required to degrade ubiquitinated proteins by the 26 S proteasome.The Journal of biological chemistry · 2013Article
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
Protein degradation by eukaryotic proteasomes is a multi-step process involving substrate recognition, ATP-dependent unfolding, translocation into the proteolytic core particle, and finally proteolysis. To date, most investigations of proteasome function have focused on the first and the last steps in this process. Here we examine the relationship between the stability of a folded protein domain and its degradation rate. Test proteins were targeted to the proteasome independently of ubiquitination by directly tethering them to the protease. Degradation kinetics were compared for test protein pairs whose stability was altered by either point mutation or ligand binding, but were otherwise identical. In both intact cells and in reactions using purified proteasomes and substrates, increased substrate stability led to an increase in substrate turnover time. The steady-state time for degradation ranged from ∼5 min (dihydrofolate reductase) to 40 min (I27 domain of titin). ATP turnover was 110/min./proteasome, and was not markedly changed by substrate. Proteasomes engage tightly folded substrates in multiple iterative rounds of ATP hydrolysis, a process that can be rate-limiting 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.