Aurora kinases are serine/threonine kinases that are essential for cell proliferation. They are phosphotransferase enzymes that help the dividing cell dispense its genetic materials to 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.[1] The first aurora kinases were identified in Drosophila melanogaster, where mutations led to failure of centrosome separation with the monopolar spindles reminiscent of the North Pole, suggesting the name aurora.[2]
Three Aurora kinases have been identified in mammalian cells to date. Besides being implicated as mitotic regulators, these three kinases have generated significant interest in the cancer research field due to their elevated expression profiles in many human cancers.[3] The human Aurora kinases present a similar domain organization, with a N-terminal domain of 39–129 residues in length, a related Ser/Thr protein kinase domain and a short C-terminal domain containing 15–20 residues. The N-terminal domain of three proteins share low sequence conservation, which determines selectivity during protein–protein interactions.[1]
As described above, there are three classes of aurora kinases in multicellular organisms, including humans:
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