Aurora kinases are serine/threonine kinases that are essential for cell proliferation. The enzyme helps the dividing cell share its genetic materials with its daughter cells. More specifically, Aurora kinases play a crucial role in cellular division by controlling chromatid segregation. Defects in this segregation can cause genetic instability, a condition which is highly associated with tumorigenesis (Bolanos-Garcia, 2005). Three Aurora kinases have been identified in mammalian cells to date. Besides being implicated as mitotic regulators, these three members of the mammalian family have generated significant interest in the cancer research field due to their elevated expression profiles in many human cancers (Giet & Prigent, 1999). The human Aurora kinases present a similar domain organization, with a N-terminal domain of 39 to 129 residues in length, a protein kinase domain and a short C-terminal domain containing 15 to 20 residues. The N-terminal domain of three proteins share low sequence conservation, which determines selectivity during protein-protein interactions (Bolanos-Garcia, 2005).
As, mentioned above, there are three classes of aurora kinases:
- Aurora A (aka Aurora 2) functions during prophase of mitosis and is required for correct function of the centrosomes (the microtubule organising centres in eukaryotic cells).
- Aurora B (aka Aurora 1) functions in the attachment of the mitotic spindle to the centromere.
- Aurora C (AURKC) works in germ-line cells and little is known about its function.
Bolanos-garcia V M. Aurora kinases. The International Journal of Biochemistry & Cell Biology 37 (2005) 1572–1577.
Giet R, Prigent C. Aurora/Ipl1p-related kinases, a new oncogenic family of mitotic serine-threonine kinases. Journal of Cell Science 112 (1999) 3591–3601.
|60x45px||This enzyme-related article is a stub. You can help Wikipedia by expanding it.|