ArticleMolecular cancer2017
BMI1, a new target of CK2α.
Article in Molecular cancer, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.
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Who cites it
17 citing papers in PubMed, 27 citations in OpenAlex.
- Plitidepsin induces apoptosis in glioma cells through β-TrCP-mediated ubiquitination and degradation of BMI1.Naunyn-Schmiedeberg's archives of pharmacology · 2026Article
- Co-delivery of cisplatin and Bmi1 siRNA via nanocapsules overcomes chemoresistance in ovarian cancer.Scientific reports · 2026Article
- CK2α-mediated phosphorylation of DUB3 promotes YAP1 stability and oncogenic functions.Cell death & disease · 2025Article
- Bmi1 deficiency exacerbates hyperoxia-induced acute lung injury in mice.Frontiers in physiology · 2025Article
- Integrated multi-omics analysis reveals the immunotherapeutic significance of tumor cells with high FN1 expression in ovarian cancer.Frontiers in molecular biosciences · 2025Article
- PP2A inhibitor SET promotes mTORC1 and Bmi1 signaling through Akt activation and maintains the colony-formation ability of cancer cells.The Journal of biological chemistry · 2024Article
- Article
- Protein kinase CK2 - diverse roles in cancer cell biology and therapeutic promise.Molecular and cellular biochemistry · 2023Review
- Post-Translational Modifications in Atopic Dermatitis: Current Research and Clinical Relevance.Frontiers in cell and developmental biology · 2022Review
- Bmi-1 alleviates adventitial fibroblast senescence by eliminating ROS in pulmonary hypertension.BMC pulmonary medicine · 2021Article
- KRCC1: A potential therapeutic target in ovarian cancer.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2020Article
- Combination chemotherapy of valproic acid (VPA) and gemcitabine regulates STAT3/Bmi1 pathway to differentially potentiate the motility of pancreatic cancer cells.Cell & bioscience · 2019Article
- The RASSF6 Tumor Suppressor Protein Regulates Apoptosis and Cell Cycle Progression via Retinoblastoma Protein.Molecular and cellular biology · 2018Article
- Targeting of BMI-1 expression by the novel small molecule PTC596 in mantle cell lymphoma.Oncotarget · 2018Article
- The Functions of MicroRNA-200 Family in Ovarian Cancer: Beyond Epithelial-Mesenchymal Transition.International journal of molecular sciences · 2017Review
- Pharmacological inhibition of Bmi1 by PTC-209 impaired tumor growth in head neck squamous cell carcinoma.Cancer cell international · 2017Article
- Reciprocal regulation between B lymphoma Mo-MLV insertion region 1 homolog and type I insulin-like growth factor receptor in pemetrexed-resistant lung cancer cells.Tzu chi medical journalArticle
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Authors and funding
7 authors at 1 institution in 1 country.
Funding
Abstract
backgroundThe polycomb group protein, BMI1 plays important roles in chromatin modification, stem cell function, DNA damage repair and mitochondrial bioenergetics. Such diverse cellular functions of BMI1 could be, in part, due to post-translational modifications, especially phosphorylation. To date, AKT has been reported as a kinase that by site specific phosphorylation of BMI1 modulates its oncogenic functions.
methodsImmunoprecipitation in conjunction with kinase assay and mass spectrometry was used to determine association with and site specific phosphorylation of BMI1 by CK2α. Functional implications of the BMI1/CK2α axis was examined in cancer cells utilizing siRNA and exogenous gene expression followed by biochemical and phenotypic studies. Correlations between expression of CK2α and BMI1 were determined from cell lines and formalin fixed paraffin embedded tissues representing the normal fallopian tube epithelium and high grade serous ovarian cancer samples.
resultsHere we report that CK2α, a nuclear serine threonine kinase, phosphorylates BMI1 at Serine 110 as determined by in-vitro/ex-vivo kinase assay and mass spectrometry. In ovarian cancer cell lines, expression of CK2α correlated with the phospho-species, as well as basal BMI1 levels. Preventing phosphorylation of BMI1 at Serine 110 significantly decreased half-life and stability of the protein. Additionally, re-expression of the phosphorylatable but not non-phosphorylatable BMI1 rescued clonal growth in endogenous BMI1 silenced cancer cells leading us to speculate that CK2α-mediated phosphorylation stabilizes BMI1 and promotes its oncogenic function. Clinically, compared to normal fallopian tube epithelial tissues, the expression of both BMI1 and CK2α were significantly higher in tumor tissues obtained from high-grade serous ovarian cancer patients. Among tumor samples, the expression of BMI1 and CK2α positively correlated (Spearman coefficient = 0.62, P = 0.0021) with each other.
conclusionTaken together, our findings establish an important regulatory role of CK2α on BMI1 phosphorylation and stability and implicate the CK2α/BMI1 axis in ovarian cancer.
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