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• W3015373377 abstract "The DNA-dependent protein kinase catalytic subunit (DNA-PKcs) has well-established roles in DNA double-strand break repair, and recently, nonrepair functions have also been reported. To better understand its cellular functions, we deleted DNA-PKcs from HeLa and A549 cells using CRISPR/Cas9. The resulting cells were radiation sensitive, had reduced expression of ataxia-telangiectasia mutated (ATM), and exhibited multiple mitotic defects. Mechanistically, nocodazole-induced upregulation of cyclin B1, anillin, and securin was decreased in DNA-PKcs-deficient cells, as were phosphorylation of Aurora A on threonine 288, phosphorylation of Polo-like kinase 1 (PLK1) on threonine 210, and phosphorylation of targeting protein for Xenopus Klp2 (TPX2) on serine 121." @default.
• W3015373377 created "2020-04-17" @default.
• W3015373377 creator A5010005294 @default.
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• W3015373377 date "2020-06-15" @default.
• W3015373377 modified "2023-10-18" @default.
• W3015373377 title "Nocodazole-Induced Expression and Phosphorylation of Anillin and Other Mitotic Proteins Are Decreased in DNA-Dependent Protein Kinase Catalytic Subunit-Deficient Cells and Rescued by Inhibition of the Anaphase-Promoting Complex/Cyclosome with proTAME but Not Apcin" @default.
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• W3015373377 doi "https://doi.org/10.1128/mcb.00191-19" @default.
• W3015373377 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/7296215" @default.
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