ArticleNature cell biology2010
Ubiquitin hydrolase Dub3 promotes oncogenic transformation by stabilizing Cdc25A.
Article in Nature cell biology, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 85 papers.
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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.
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Who cites it
85 citing papers in PubMed, 120 citations in OpenAlex.
- Assessment of USP17 and TPT1 Expression in Primary and Matched Metastatic Tissue of Patients with High-Grade Serous Ovarian Carcinoma and the Relationship to Distant Metastasis.Diagnostics (Basel, Switzerland) · 2026Article
- Locus-specific proteomics identifies novel regulators of Epstein-Barr virus lytic reactivation.Journal of virology · 2026Article
- The deubiquitinase USP17 regulates the expression and activity of the oncogenic driver β-catenin in colorectal cancer.Oncogene · 2026Article
- TDP-43/ALKBH5-mediated mMedComm · 2025Article
- Deubiquitinases and Cancer.Journal of pharmacy & bioallied sciences · 2024Review
- Review
- DUB3 is a MAGEA3 deubiquitinase and a potential therapeutic target in hepatocellular carcinoma.iScience · 2024Article
- mInternational journal of biological sciences · 2024Article
- Deubiquitylating Enzymes in Cancer and Immunity.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2023Review
- The Role of Deubiquitinating Enzyme in Head and Neck Squamous Cell Carcinoma.International journal of molecular sciences · 2022Review
- Renal Cell Carcinoma as a Metabolic Disease: An Update on Main Pathways, Potential Biomarkers, and Therapeutic Targets.International journal of molecular sciences · 2022Review
- Review
- Deubiquitinases in cell death and inflammation.The Biochemical journal · 2022Review
- USP17 is required for peripheral trafficking of lysosomes.EMBO reports · 2022Article
- DUB3/KLF4 combats tumor growth and chemoresistance in hepatocellular carcinoma.Cell death discovery · 2022Article
- The role of the deubiquitinating enzyme DUB3/USP17 in cancer: a narrative review.Cancer cell international · 2021Review
- Ubiquitin-Specific Protease 29 Regulates Cdc25A-Mediated Tumorigenesis.International journal of molecular sciences · 2021Article
- Cellular and Molecular Mechanisms of Pristimerin in Cancer Therapy: Recent Advances.Frontiers in oncology · 2021Review
- Ubiquitination and deubiquitination of MCL1 in cancer: deciphering chemoresistance mechanisms and providing potential therapeutic options.Cell death & disease · 2020Review
- Skeletal muscle transcriptional networks linked to type I myofiber grouping in Parkinson's disease.Journal of applied physiology (Bethesda, Md. : 1985) · 2020Article
25 more citing papers are in PubMed but not listed here.
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Authors and funding
8 authors at 3 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The dual specificity (Tyr/Thr) phosphatase Cdc25A activates cyclin-dependent kinases (Cdks) to promote cell-cycle progression and has significant oncogenic potential. Cdc25A protein levels are regulated tightly in normal tissues, but many human cancers overexpress Cdc25A. The underlying mechanism for overexpression has been enigmatic. Here we show that Cdc25A is stabilized by the ubiquitin hydrolase Dub3. Upon binding Cdc25A, Dub3 removes the polyubiquitin modifications that mark Cdc25A for proteasomal degradation. Dub3 knockdown in cells increased Cdc25A ubiquitylation and degradation, resulting in reduced Cdk/Cyclin activity and arrest at G1/S and G2/M phases of the cell cycle. In contrast, acute Dub3 overexpression produced a signature response to oncogene induction: cells accumulated in S and G2 because of replication stress, and activated a DNA damage response. Dub3 also transformed NIH-3T3 cells and cooperated with activated H-Ras to promote growth in soft agar. Importantly, we show that Dub3 overexpression is responsible for an abnormally high level of Cdc25A in a subset of human breast cancers. Moreover, Dub3 knockdown significantly retarded the growth of breast tumour xenografts in nude mice. As a major regulator of Cdc25A, Dub3 is an example of a transforming ubiquitin hydrolase that subverts a key component of the cell cycle machinery.
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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.