ArticleOncotarget2013
DNA damage-induced ubiquitylation of proteasome controls its proteolytic activity.
Article in Oncotarget, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 37 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
37 citing papers in PubMed, 55 citations in OpenAlex.
- The role of HECT-type E3 ubiquitin ligases in DNA damage response and repair.Cell death discovery · 2025Review
- PSMA5 as a modulator of glioblastoma senescence and prognosis.BMC cancer · 2025Article
- Ubiquitin recruiting chimera: more than just a PROTAC.Biology direct · 2024Review
- Glucose restriction in Saccharomyces cerevisiae modulates the phosphorylation pattern of the 20S proteasome and increases its activity.Scientific reports · 2023Article
- Identification of Potentially Novel Molecular Targets of Endometrial Cancer Using a Non-Biased Proteomic Approach.Cancers · 2023Article
- p53 Affects Zeb1 Interactome of Breast Cancer Stem Cells.International journal of molecular sciences · 2023Article
- The genomic landscape of ANCA-associated vasculitis: Distinct transcriptional signatures, molecular endotypes and comparison with systemic lupus erythematosus.Frontiers in immunology · 2023Article
- Retinoic acid regulates the ubiquitin-proteasome system in a middle cerebral artery occlusion animal model.Laboratory animal research · 2022Article
- DNA damage and regulation of protein homeostasis.DNA repair · 2021Review
- Cleavage of the APE1 N-Terminal Domain in Acute Myeloid Leukemia Cells Is Associated with Proteasomal Activity.Biomolecules · 2020Article
- ANLN Directly Interacts with RhoA to Promote Doxorubicin Resistance in Breast Cancer Cells.Cancer management and research · 2020Article
- Attenuation of p53 mutant as an approach for treatment Her2-positive cancer.Cell death discovery · 2020Review
- Suppression of the Ubiquitin Pathway by Small Molecule Binding to Ubiquitin Enhances Doxorubicin Sensitivity of the Cancer Cells.Molecules (Basel, Switzerland) · 2019Article
- Article
- Identification of proteins differentially expressed by glutamate treatment in cerebral cortex of neonatal rats.Laboratory animal research · 2019Article
- Positioning of proteasome inhibitors in therapy of solid malignancies.Cancer chemotherapy and pharmacology · 2018Review
- Combined treatment of human multiple myeloma cells with bortezomib and doxorubicin alters the interactome of 20S proteasomes.Cell cycle (Georgetown, Tex.) · 2018Article
- Novel isatin-derived molecules activate p53 via interference with Mdm2 to promote apoptosis.Cell cycle (Georgetown, Tex.) · 2018Article
- Proteomic analysis of affinity-purified extracellular proteasomes reveals exclusively 20S complexes.Oncotarget · 2017Article
- One-carbon metabolism and nucleotide biosynthesis as attractive targets for anticancer therapy.Oncotarget · 2017Review
Corrections and comments
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Authors and funding
4 authors at 3 institutions in 4 countries.
Funding
Abstract
Stability of proteins is largely controlled by post-translational covalent modifications. Among those, ubiquitylation plays a central role as it marks the proteins for proteasome-dependent degradation. Proteolytic activities of proteasomes are critical for execution of various cellular processes, including DNA damage signaling and repair. However, very little is known about the regulation of proteasomal activity in cells during genotoxic stress. Here we investigated post-translational modifications of the 20S proteasomal subunits upon DNA damage induced by doxorubicin. Using mass-spectrometry, we found novel sites of phosphorylation and ubiquitylation in multiple proteasome subunits upon doxorubicin treatment. Ectopic co-expression of proteasome subunits and tagged ubiquitin confirmed the presence of ubiquitylated forms of PSMA5, PSMA1, PSMA3 and PSMB5 in cells. Moreover, we demonstrated that ubiquitylation in vitro inhibited chymotrypsin-like and caspase-like activities of proteasomes. In vivo, doxorubicin increased the activity of proteasomes, paralleling with attenuation of the overall level of proteasome ubiquitylation. Collectively, our results suggest a novel mechanism whereby the proteolytic activities of proteasomes are dynamically regulated by ubiquitylation upon DNA damage.
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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.