ArticleACS chemical biology2011
Proteasomal degradation from internal sites favors partial proteolysis via remote domain stabilization.
Article in ACS chemical biology, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.
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Who cites it
21 citing papers in PubMed, 31 citations in OpenAlex.
- Mechanisms and regulation of substrate degradation by the 26S proteasome.Nature reviews. Molecular cell biology · 2025Review
- Substrate-specific effects of natural genetic variation on proteasome activity.PLoS genetics · 2023Article
- FtsH degrades kinetically stable dimers of cyclopropane fatty acid synthase via an internal degron.Molecular microbiology · 2023Article
- Combinatorial and antagonistic effects of tubulin glutamylation and glycylation on katanin microtubule severing.Developmental cell · 2022Article
- Review
- Targeted substrate loop insertion by VCP/p97 during PP1 complex disassembly.Nature structural & molecular biology · 2021Article
- Structure, Dynamics and Function of the 26S Proteasome.Sub-cellular biochemistry · 2021Review
- Article
- Structure and Function of the 26S Proteasome.Annual review of biochemistry · 2018Review
- Substrate Ubiquitination Controls the Unfolding Ability of the Proteasome.The Journal of biological chemistry · 2016Article
- Ubiquitin-like domains can target to the proteasome but proteolysis requires a disordered region.The EMBO journal · 2016Article
- Conserved Sequence Preferences Contribute to Substrate Recognition by the Proteasome.The Journal of biological chemistry · 2016Article
- Sequence composition of disordered regions fine-tunes protein half-life.Nature structural & molecular biology · 2015Article
- VWA domain of S5a restricts the ability to bind ubiquitin and Ubl to the 26S proteasome.Molecular biology of the cell · 2014Article
- Disordered proteinaceous machines.Chemical reviews · 2014Review
- Measuring activity in the ubiquitin-proteasome system: from large scale discoveries to single cells analysis.Cell biochemistry and biophysics · 2013Review
- Article
- Article
- Sequence- and species-dependence of proteasomal processivity.ACS chemical biology · 2012Article
- A three-part signal governs differential processing of Gli1 and Gli3 proteins by the proteasome.The Journal of biological chemistry · 2011Article
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
The ubiquitin-proteasome system controls the concentrations of hundreds of regulatory proteins and removes misfolded and damaged proteins in eukaryotic cells. The proteasome recognizes ubiquitinated proteins and then engages its substrates at unstructured initiation regions. After initiation, it proceeds along the polypeptide chain, unraveling folded domains sequentially and degrading the protein completely. In vivo the proteasome can, and likely often does, initiate degradation at internal sites within its substrates, but it is not known how this affects the outcome of the degradation reaction. Here we find that domains flanking the initiation region can protect each other against degradation without interacting directly. The magnitude of this effect is related to the stability of both domains and can be tuned from complete degradation to complete protection of one domain. Partial proteasomal degradation has been observed in the cell in three signaling pathways and is associated with internal initiation. Thus, the basic biochemical mechanism of remote stabilization of protein domains is important in proteasome biology.
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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.