The DOI matches its Crossref record; 3 of the 3 references it cites were found in a registry or an index.
The functional diversity of Aurora kinases: a comprehensive review
Open accessAbstract
Aurora kinases are serine/threonine kinases essential for the onset and progression of mitosis. Aurora members share a similar protein structure and kinase activity, but exhibit distinct cellular and subcellular localization. AurA favors the G2/M transition by promoting centrosome maturation and mitotic spindle assembly. AurB and AurC are chromosome-passenger complex proteins, crucial for chromosome binding to kinetochores and segregation of chromosomes. Cellular distribution of AurB is ubiquitous, while AurC expression is mainly restricted to meiotically-active germ cells. In human tumors, all Aurora kinase members play oncogenic roles related to their mitotic activity and promote cancer cell survival and proliferation. Furthermore, AurA plays tumor-promoting roles unrelated to mitosis, including tumor stemness, epithelial-to-mesenchymal transition and invasion. In this review, we aim to understand the functional interplay of Aurora kinases in various types of human cells, including tumor cells. The understanding of the functional diversity of Aurora kinases could help to evaluate their relevance as potential therapeutic targets in cancer.
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The bipolar mitotic kinesin Eg5 moves on both microtubules that it crosslinks
Kapitein, L. C., Peterman, E. J. G., Kwok, B. H., Kim, J. H., Kapoor, T. M., & Schmidt, C. F. (2005) · Nature · doi:10.1038/nature03503 · Cited by 678
Aurora A phosphorylates MCAK to control ran-dependent spindle bipolarity
Zhang, X., Ems-McClung, S. C., & Walczak, C. E. (2008) · Molecular Biology of the Cell · doi:10.1091/mbc.e08-02-0198 · Cited by 123
Plk1 and Aurora A regulate the depolymerase activity and the cellular localization of Kif2a
Jang, C.-Y., Coppinger, J. A., Seki, A., Yates, J. R., & Fang, G. (2009) · Journal of Cell Science · doi:10.1242/jcs.044321 · Cited by 99
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Beurois, J., Cazin, C., Kherraf, Z.-E., Martinez, G., Celse, T., Touré, A., Arnoult, C., Ray, P. F., & Coutton, C. (2020) · Best Practice & Research Clinical Endocrinology & Metabolism · doi:10.1016/j.beem.2020.101473 · Cited by 71
Development of covalent inhibitors: Principle, design, and application in cancer
Zheng, L., Li, Y., Wu, D., Xiao, H., Zheng, S., Wang, G., & Sun, Q. (2023) · MedComm – Oncology · doi:10.1002/mog2.56 · Cited by 71
Cyclers’ kinases in cell division: from molecules to cancer therapy
Milletti, G., Colicchia, V., & Cecconi, F. (2023) · Cell Death & Differentiation · doi:10.1038/s41418-023-01196-z · Cited by 39
Blazejewski, S. M., Bennison, S. A., Liu, X., & Toyo-oka, K. (2021) · Scientific Reports · doi:10.1038/s41598-021-87521-3 · Cited by 27
Metadata
- Authors
- Willems, E., Dedobbeleer, M., Digregorio, M., Lombard, A., Lumapat, P. N., & Rogister, B.
- Venue
- Cell Division
- Published
- 2018-09-19
- Volume
- 13
- Issue
- 1
- Pages
- 7-7
- ISSN
- 1747-1028 (ISSN-L)
- OpenAlex
- W2891127847
- Cited by
- 416
- References
- 3
- FWCI
- 14.98
- Type
- journal article
- Language
- en
- Open access
- gold
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