ArticleCell death & disease2017
WDR79 promotes the proliferation of non-small cell lung cancer cells via USP7-mediated regulation of the Mdm2-p53 pathway.
Article in Cell death & disease, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.
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Who cites it
19 citing papers in PubMed, 28 citations in OpenAlex.
- USP7 at PML Nuclear Bodies: A Protein Interaction Network Perspective.International journal of molecular sciences · 2026Article
- Emerging roles of USP7 in tumor immune evasion, metabolic reprogramming, and therapeutic resistance.Frontiers in immunology · 2026Review
- Biomolecular condensates in lung cancer: from molecular mechanisms to therapeutic targeting.Cell death discovery · 2025Review
- Pseudokinase TRIB3 stabilizes SSRP1 via USP10-mediated deubiquitination to promote multiple myeloma progression.Oncogene · 2025Article
- The role of m6A demethylases in lung cancer: diagnostic and therapeutic implications.Frontiers in immunology · 2023Review
- Differential effects of WRAP53 transcript variants on non-small cell lung cancer cell behaviors.PloS one · 2023Article
- WDR79 promotes aerobic glycolysis of pancreatic ductal adenocarcinoma (PDAC) by the suppression of SIRT4.Open medicine (Warsaw, Poland) · 2023Article
- Unraveling the Complex Interactions between the Fat Mass and Obesity-Associated (FTO) Gene, Lifestyle, and Cancer.Advances in nutrition (Bethesda, Md.) · 2022Review
- The Role of WRAP53 in Cell Homeostasis and Carcinogenesis Onset.Current issues in molecular biology · 2022Review
- Regulation of Cancer Metabolism by Deubiquitinating Enzymes: The Warburg Effect.International journal of molecular sciences · 2021Review
- Article
- Combination of Inhibitors of USP7 and PLK1 has a Strong Synergism against Paclitaxel Resistance.International journal of molecular sciences · 2020Article
- Stabilization of the histone acetyltransferase Tip60 by deubiquitinating enzyme USP7 stimulates the release of pro-inflammatory mediators in acute lung injury.Journal of molecular medicine (Berlin, Germany) · 2020Article
- IU1 suppresses proliferation of cervical cancer cells through MDM2 degradation.International journal of biological sciences · 2020Article
- PTEN downregulates WD repeat‑containing protein 66 in salivary adenoid cystic carcinoma.Oncology reports · 2019Article
- Expression of WDR79 is associated withJournal of Cancer · 2019Article
- WDR79 mediates the proliferation of non-small cell lung cancer cells by regulating the stability of UHRF1.Journal of cellular and molecular medicine · 2018Article
- Clinical Significance of Ubiquitin Specific Protease 7 (USP7) in Predicting Prognosis of Hepatocellular Carcinoma and its Functional Mechanisms.Medical science monitor : international medical journal of experimental and clinical research · 2018Article
- Emerging insights into HAUSP (USP7) in physiology, cancer and other diseases.Signal transduction and targeted therapyArticle
Corrections and comments
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Authors and funding
12 authors at 4 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
WD repeat protein 79 (WDR79) is a member of the WD-repeat protein family and functions as a scaffold protein during telomerase assembly, Cajal body formation and DNA double strand break repair. We have previously shown that WDR79 is frequently overexpressed in cell lines and tissues derived from non-small cell lung cancer (NSCLC) and it accelerates cell proliferation in NSCLC. However, the detailed mechanism underlying the role of WDR79 in the proliferation of NSCLC cells remains unclear. Here, we report the discovery of a molecular interaction between WDR79 and USP7 and show its functional significance in linking the Mdm2-p53 pathway to the proliferation of NSCLC cells. We found that WDR79 colocalized and interacted with USP7 in the nucleus of NSCLC cells. This event, in turn, reduced the ubiquitination of Mdm2 and p53, thereby increasing the stability and extending the half-life of the two proteins. We further found that the functional effects of WDR79 depended upon USP7, because the knockdown of USP7 resulted in their attenuation. Finally, we demonstrated that WDR79 promoted the proliferation of NSCLC cells via USP7. Taken together, our findings reveal a novel molecular function of WDR79 and may lead to broadly applicable and innovative therapeutic avenues for NSCLC.
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