ArticleNature chemical biology2009
Substrate selection by the proteasome during degradation of protein complexes.
Article in Nature chemical biology, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 63 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.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
63 citing papers in PubMed, 116 citations in OpenAlex.
- The local mechanostructural properties of protein cargoes regulate nucleocytoplasmic transport.Nature physics · 2026Article
- Molecular features defining the efficiency of bioPROTACs.Communications biology · 2025Article
- Emergence and Enhancement of Ultrasensitivity through Posttranslational Modulation of Protein Stability.Biomolecules · 2021Article
- Article
- Structure, Dynamics and Function of the 26S Proteasome.Sub-cellular biochemistry · 2021Review
- Genetic Selection Based on a Ste6G3 (Bethesda, Md.) · 2020Article
- A technique for delineating the unfolding requirements for substrate entry into retrotranslocons during endoplasmic reticulum-associated degradation.The Journal of biological chemistry · 2019Article
- Disordered region of cereblon is required for efficient degradation by proteolysis-targeting chimera.Scientific reports · 2019Article
- Substrate selection by the proteasome through initiation regions.Protein science : a publication of the Protein Society · 2019Review
- Melting Down Protein Stability: PAPS Synthase 2 in Patients and in a Cellular Environment.Frontiers in molecular biosciences · 2019Review
- The antizyme family for regulating polyamines.The Journal of biological chemistry · 2018Review
- Structure and Function of the 26S Proteasome.Annual review of biochemistry · 2018Review
- Biological and Pathological Implications of an Alternative ATP-Powered Proteasomal Assembly With Cdc48 and the 20S Peptidase.Frontiers in molecular biosciences · 2018Review
- The Atypical Ubiquitin E2 Conjugase UBE2L3 Is an Indirect Caspase-1 Target and Controls IL-1β Secretion by Inflammasomes.Cell reports · 2017Article
- An N-end rule pathway that recognizes proline and destroys gluconeogenic enzymes.Science (New York, N.Y.) · 2017Article
- The contribution of intrinsically disordered regions to protein function, cellular complexity, and human disease.Biochemical Society transactions · 2016Review
- The Deubiquitinase USP47 Stabilizes MAPK by Counteracting the Function of the N-end Rule ligase POE/UBR4 in Drosophila.PLoS biology · 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
- The Proteasome Subunit Rpn8 Interacts with the Small Nucleolar RNA Protein (snoRNP) Assembly Protein Pih1 and Mediates Its Ubiquitin-independent Degradation in Saccharomyces cerevisiae.The Journal of biological chemistry · 2016Article
3 more citing papers are in PubMed but not listed here.
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
The proteasome controls the turnover of many cellular proteins. Two structural features are typically required for proteins to be degraded: covalently attached ubiquitin polypeptides that allow binding to the proteasome and an unstructured region in the targeted protein that initiates proteolysis. Here, we have tested the degradation of model proteins to further explore how the proteasome selects its substrates. Using purified yeast proteasome and mammalian proteasome in cell lysate, we have demonstrated that the two structural features can act in trans when separated onto different proteins in a multisubunit complex. In such complexes, the location of the unstructured initiation site and its chemical properties determine which subunit is degraded. Thus, our findings reveal the molecular basis of subunit specificity in the degradation of protein complexes. In addition, our data provide a plausible explanation for how adaptor proteins can bind to otherwise stable proteins and target them for degradation.
Indexed as
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What OpenQuestion holds
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.