ArticleACS chemical biology2012
Sequence- and species-dependence of proteasomal processivity.
Article in ACS chemical biology, 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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Who cites it
40 citing papers in PubMed.
- Pulling and gripping: Proteasomal translocation pathway elements differentially contribute to substrate unfolding.Protein science : a publication of the Protein Society · 2026Article
- Missense substitutions in the BTB domain of ZBTB24 can lead to protein instability and cause ICF2 syndrome.Human molecular genetics · 2026Article
- Real-time capture of σNature communications · 2025Article
- Modeling liquid-liquid phase separation and its impact on proteasomal substrate degradation.Computational and structural biotechnology journal · 2025Article
- How the double-ring ClpAP protease motor grips the substrate to unfold and degrade stable proteins.The Journal of biological chemistry · 2024Article
- Slippery sequences stall the 26S proteasome at multiple points along the translocation pathway.Protein science : a publication of the Protein Society · 2024Article
- Substrate-specific effects of natural genetic variation on proteasome activity.PLoS genetics · 2023Article
- AAA+ protease-adaptor structures reveal altered conformations and ring specialization.Nature structural & molecular biology · 2022Article
- Single molecule microscopy reveals diverse actions of substrate sequences that impair ClpX AAA+ ATPase function.The Journal of biological chemistry · 2022Article
- Proteasomal conformation controls unfolding ability.Proceedings of the National Academy of Sciences of the United States of America · 2021Article
- Mechanisms of substrate recognition by the 26S proteasome.Current opinion in structural biology · 2021Review
- Structure, Dynamics and Function of the 26S Proteasome.Sub-cellular biochemistry · 2021Review
- Mode of targeting to the proteasome determines GFP fate.The Journal of biological chemistry · 2020Article
- Mitochondrial ClpX activates an essential biosynthetic enzyme through partial unfolding.eLife · 2020Article
- The proteasome 19S cap and its ubiquitin receptors provide a versatile recognition platform for substrates.Nature communications · 2020Article
- Ubiquitin receptors are required for substrate-mediated activation of the proteasome's unfolding ability.Scientific reports · 2019Article
- Article
- Tandem Fluorescent Protein Timers for Noninvasive Relative Protein Lifetime Measurement in Plants.Plant physiology · 2019Article
- Article
- Structure and Function of the 26S Proteasome.Annual review of biochemistry · 2018Review
Corrections and comments
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Authors and funding
8 authors.
Funding
Abstract
The proteasome is the degradation machine at the center of the ubiquitin-proteasome system and controls the concentrations of many proteins in eukaryotes. It is highly processive so that substrates are degraded completely into small peptides, avoiding the formation of potentially toxic fragments. Nonetheless, some proteins are incompletely degraded, indicating the existence of factors that influence proteasomal processivity. We have quantified proteasomal processivity and determined the underlying rates of substrate degradation and release. We find that processivity increases with species complexity over a 5-fold range between yeast and mammalian proteasome, and the effect is due to slower but more persistent degradation by proteasomes from more complex organisms. A sequence stretch that has been implicated in causing incomplete degradation, the glycine-rich region of the NFκB subunit p105, reduces the proteasome's ability to unfold its substrate, and polyglutamine repeats such as found in Huntington's disease reduce the processivity of the proteasome in a length-dependent manner.
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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.