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Updated: May 24, 2026

A Guide to Production, Crystallization, and Structure Determination of Human IKK1/α
Published on: November 2, 2018
Cdc25A promotes cell survival by stimulating NF-κB activity through IκB-α phosphorylation and destabilization
Hey-Young Hong1, Jiyeon Choi, Young-Wook Cho
1Department of Biochemistry, College of Natural Sciences, Kangwon National University, 192-1 Hyoja-2-dong, Chuncheon 200-701, Republic of Korea.
Abstract:
Cell division cycle 25A (Cdc25A), a dual specificity protein phosphatase, exhibits anti-apoptotic activity, but the underlying molecular mechanisms are poorly characterized. Here we report that Cdc25A inhibits cisplatin-induced apoptotic cell death by stimulating nuclear factor-kappa B (NF-κB) activity. In HEK-293 cells, Cdc25A decreased protein level of inhibitor subunit kappa B alpha (Iκ-Bα) in association with increased serine 32-phosphorylation, followed by stimulation of transcriptional activity of NF-κB. Inhibition of NF-κB activity by chemical inhibitor or overexpression of Iκ-Bα in Cdc25A-elevated cancer cells resistant to cisplatin improved their sensitivity to cisplatin-induced apoptosis. Our data show for the first time that Cdc25A has an important physiological role in NF-κB activity regulation and it may be an important survival mechanism of cancer cells.
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