ArticleMolecular cancer research : MCR2013
Dysregulating IRES-dependent translation contributes to overexpression of oncogenic Aurora A Kinase.
Article in Molecular cancer research : MCR, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers, 1 of them a synthesis that pooled it.
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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
15 citing papers in PubMed, 1 synthesis or guideline pooled it, 32 citations in OpenAlex.
- Pooled it
- HNRNPH1-mediated splicing events regulatebioRxiv : the preprint server for biology · 2025Article
- Differential translation of mRNA isoforms underlies oncogenic activation of cell cycle kinase Aurora A.eLife · 2023Article
- Internal ribosomal entry site-mediated translational activity of nitric oxide synthase 2.Animal cells and systems · 2023Article
- Regulating the regulator: a survey of mechanisms from transcription to translation controlling expression of mammalian cell cycle kinase Aurora A.Open biology · 2022Review
- Aurora kinase A inhibitor, LY3295668 erbumine: a phase 1 monotherapy safety study in patients with locally advanced or metastatic solid tumors.Investigational new drugs · 2021Article
- The MAPK and AMPK signalings: interplay and implication in targeted cancer therapy.Journal of hematology & oncology · 2020Review
- The E3 ubiquitin ligase TRIP12 participates in cell cycle progression and chromosome stability.Scientific reports · 2020Article
- Translational control of the undifferentiated phenotype in ER‑positive breast tumor cells: Cytoplasmic localization of ERα and impact of IRES inhibition.Oncology reports · 2018Article
- A researcher's guide to the galaxy of IRESs.Cellular and molecular life sciences : CMLS · 2017Review
- Translational upregulation of Aurora-A by hnRNP Q1 contributes to cell proliferation and tumorigenesis in colorectal cancer.Cell death & disease · 2017Article
- Translational Dysregulation in Cancer: Molecular Insights and Potential Clinical Applications in Biomarker Development.Frontiers in oncology · 2017Review
- IRES-dependent translation of the long non coding RNA meloe in melanoma cells produces the most immunogenic MELOE antigens.Oncotarget · 2016Article
- Evolving Lessons on the Complex Role of AMPK in Normal Physiology and Cancer.Trends in pharmacological sciences · 2016Review
- Small molecule inhibitors of IRES-mediated translation.Cancer biology & therapy · 2015Article
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
unlabelledOverexpression of the oncoprotein Aurora A kinase occurs in multiple types of cancer, often early during cell transformation. To identify the mechanism(s) contributing to enhanced Aurora A protein expression, a comparison between normal human lung fibroblast and breast epithelial cells to nontumorigenic breast (MCF10A and MCF12A) and tumorigenic breast (MCF-7) and cervical cell lines (HeLa S3) was performed. A subset of these immortalized lines (MCF10A, MCF12A, and HeLa S3) exhibited increased levels of Aurora A protein, independent of tumorigenicity. The increase in Aurora A protein in these immortalized cells was not due to increased transcription/RNA stability, protein half-life, or cap-dependent translation. Assays utilizing monocistronic and dicistronic RNA constructs revealed that the 5'-leader sequence of Aurora A contains an internal ribosomal entry site (IRES), which is regulated in a cell cycle-dependent manner, peaking in G2/M phase. Moreover, IRES activity was increased in the immortalized cell lines in which Aurora A protein expression was also enhanced. Additional studies indicated that the increased internal initiation is specific to the IRES of Aurora A and may be an early event during cancer progression. These results identify a novel mechanism contributing to Aurora A kinase overexpression. IMPLICATIONS: The current study indicates that Aurora A kinase contributes to immortalization and tumorigenesis.
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