ArticleOncogene2010
Dual-specificity phosphatase 26 is a novel p53 phosphatase and inhibits p53 tumor suppressor functions in human neuroblastoma.
Article in Oncogene, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 papers.
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Who cites it
31 citing papers in PubMed, 56 citations in OpenAlex.
- DUSP family phosphatases in cell signaling, inflammation, and chronic diseases.Journal of biomedical science · 2026Review
- DUSP26: Unveiling a critical molecular mediator and therapeutic target in developmental dysplasia of the hip‑associated secondary osteoarthritis.International journal of molecular medicine · 2026Article
- Maintaining Genome Integrity: Protein Kinases and Phosphatases Orchestrate the Balancing Act of DNA Double-Strand Breaks Repair in Cancer.International journal of molecular sciences · 2023Review
- Dusp26 phosphatase regulates mitochondrial respiration and oxidative stress and protects neuronal cell death.Cellular and molecular life sciences : CMLS · 2022Article
- A Review of DUSP26: Structure, Regulation and Relevance in Human Disease.International journal of molecular sciences · 2021Review
- Male-biased aganglionic megacolon in the TashT mouse model of Hirschsprung disease involves upregulation of p53 protein activity and Ddx3y gene expression.PLoS genetics · 2020Article
- MYCN amplification and ATRX mutations are incompatible in neuroblastoma.Nature communications · 2020Article
- Upregulation of DUSP14 Affects Proliferation, Invasion and Metastasis, Potentially via Epithelial-Mesenchymal Transition and Is Associated with Poor Prognosis in Pancreatic Cancer.Cancer management and research · 2020Article
- SCF(FBXW7)-mediated degradation of p53 promotes cell recovery after UV-induced DNA damage.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2019Article
- Dual-Specificity Phosphatases in Neuroblastoma Cell Growth and Differentiation.International journal of molecular sciences · 2019Review
- Review
- Copy number changes at 8p11-12 predict adverse clinical outcome and chemo- and radiotherapy response in breast cancer.Oncotarget · 2018Article
- NEAP/DUSP26 suppresses receptor tyrosine kinases and regulates neuronal development in zebrafish.Scientific reports · 2017Article
- Role of miRNAs in the pathogenesis and susceptibility of diabetes mellitus.Journal of human genetics · 2017Review
- Protein serine/threonine phosphatase PPEF-1 suppresses genotoxic stress response via dephosphorylation of PDCD5.Scientific reports · 2017Article
- Novel MDM2 inhibitor SAR405838 (MI-773) induces p53-mediated apoptosis in neuroblastoma.Oncotarget · 2016Article
- The role of the p53 tumor suppressor in metabolism and diabetes.The Journal of endocrinology · 2016Review
- Comprehensive protein tyrosine phosphatase mRNA profiling identifies new regulators in the progression of glioma.Acta neuropathologica communications · 2016Article
- Structural Insight into the Critical Role of the N-Terminal Region in the Catalytic Activity of Dual-Specificity Phosphatase 26.PloS one · 2016Article
- NSC-87877 inhibits DUSP26 function in neuroblastoma resulting in p53-mediated apoptosis.Cell death & disease · 2015Article
Corrections and comments
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Authors and funding
18 authors at 2 institutions in 1 country.
Funding
Abstract
Chemoresistance is a major cause of treatment failure and poor outcome in neuroblastoma. In this study, we investigated the expression and function of dual-specificity phosphatase 26 (DUSP26), also known as mitogen-activated protein kinase phophatase-8, in human neuroblastoma. We found that DUSP26 was expressed in a majority of neuroblastoma cell lines and tissue specimens. Importantly, we found that DUSP26 promotes the resistance of human neuroblastoma to doxorubicin-induced apoptosis by acting as a p53 phosphatase to downregulate p53 tumor suppressor function in neuroblastoma cells. Inhibiting DUSP26 expression in the IMR-32 neuroblastoma cell line enhanced doxorubicin-induced p53 phosphorylation at Ser20 and Ser37, p21, Puma, Bax expression as well as apoptosis. In contrast, DUSP26 overexpression in the SK-N-SH cell line inhibited doxorubicin-induced p53 phosphorylation at Ser20 and Ser37, p21, Puma, Bax expression and apoptosis. Using in vitro and in vivo assays, we found that DUSP26 binds to p53 and dephosphorylates p53 at Ser20 and Ser37. In this report, we show that DUSP26 functions as a p53 phosphatase, which suppresses downstream p53 activity in response to genotoxic stress. This suggests that inhibition of this phosphatase may increase neuroblastoma chemosensitivity and DUSP26 is a novel therapeutic target for this aggressive pediatric malignancy.
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