The DOI matches its Crossref record; 1 of the 1 references it cites were found in a registry or an index.
Phosphorylation of CDC25B by Aurora-A at the centrosome contributes to the G2–M transition
Open accessAbstract
Aurora-A protein kinase, which is the product of an oncogene, is required for the assembly of a functional mitotic apparatus and the regulation of cell ploidy. Overexpression of Aurora-A in tumour cells has been correlated with cancer susceptibility and poor prognosis. Aurora-A activity is required for the recruitment of CDK1-cyclin B1 to the centrosome prior to its activation and the commitment of the cell to mitosis. In this report, we demonstrate that the CDC25B phosphatase, an activator of cyclin dependent kinases at mitosis, is phosphorylated both in vitro and in vivo by Aurora-A on serine 353 and that this phosphorylated form of CDC25B is located at the centrosome during mitosis. Knockdown experiments by RNAi confirm that the centrosome phosphorylation of CDC25B on S353 depends on Aurora-A kinase. Microinjection of antibodies against phosphorylated S353 results in a mitotic delay whilst overexpression of a S353 phosphomimetic mutant enhances the mitotic inducing effect of CDC25B. Our results demonstrate that Aurora-A phosphorylates CDC25B in vivo at the centrosome during mitosis. This phosphorylation might locally participate in the control of the onset of mitosis. These findings re-emphasise the role of the centrosome as a functional integrator of the pathways contributing to the triggering of mitosis.
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Citations
Cites
Centrosome-dependent exit of cytokinesis in animal cells
Piel, M., Nordberg, J., Euteneuer, U., & Bornens, M. (2001) · Science · doi:10.1126/science.1057330 · Cited by 389
Cited by
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Marumoto, T., Zhang, D., & Saya, H. (2005) · Nature Reviews Cancer · doi:10.1038/nrc1526 · Cited by 697
Targeting AURKA in Cancer: molecular mechanisms and opportunities for Cancer therapy
Du, R., Huang, C., Liu, K., Li, X., & Dong, Z. (2021) · Molecular Cancer · doi:10.1186/s12943-020-01305-3 · Cited by 586
Shared and separate functions of polo-like kinases and aurora kinases in cancer
Lens, S. M. A., Voest, E. E., & Medema, R. H. (2010) · Nature Reviews Cancer · doi:10.1038/nrc2964 · Cited by 597
Aurora A kinase (AURKA) in normal and pathological cell division
Nikonova, A. S., Astsaturov, I., Serebriiskii, I. G., Dunbrack, R. L., & Golemis, E. A. (2013) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-012-1073-7 · Cited by 448
Metadata
- Authors
- Dutertre, S., Cazales, M., Quaranta, M., Froment, C., Trabut, V., Dozier, C., Mirey, G., Bouché, J.-P., Theis-Febvre, N., Schmitt, E., Monsarrat, B., Prigent, C., & Ducommun, B.
- Venue
- Journal of Cell Science
- Publisher
- The Company of Biologists
- Published
- 2004-05-15
- Volume
- 117
- Issue
- 12
- Pages
- 2523-2531
- ISSN
- 0021-9533 (ISSN-L)
- 1477-9137
- OpenAlex
- W2100521311
- Cited by
- 284
- References
- 1
- FWCI
- 6.77
- Type
- journal article
- Language
- en
- Open access
- green
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- Dutertre, S., Cazales, M., Quaranta, M., Froment, C., Trabut, V., Dozier, C., Mirey, G., Bouché, J.-P., Theis-Febvre, N., Schmitt, E., Monsarrat, B., Prigent, C., & Ducommun, B. (2004). Phosphorylation of CDC25B by Aurora-A at the centrosome contributes to the G2–M transition. Journal of Cell Science. https://doi.org/10.1242/jcs.01108
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