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:

See also


  1. ^ a b Bolanos-Garcia V M. Aurora kinases. The International Journal of Biochemistry & Cell Biology 37 (2005) 1572–1577.
  2. ^ Fu, Jingyan (January 2007). "Roles of Aurora Kinases in Mitosis and Tumorigenesis" (PDF). Molecular Cancer Research. 5 (1): 1. doi:10.1158/1541-7786.MCR-06-0208. PMID 17259342. Retrieved 7 February 2022.
  3. ^ 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.
  4. ^ Eyers PA, Erikson E, Chen LG, Eyers PA (April 2003). "A novel mechanism for activation of the protein kinase Aurora A". Current Biology. 13 (8): 691–697. doi:10.1016/s0960-9822(03)00166-0. PMID 12699628.
  5. ^ Bayliss R, Sardon T, Vernos I, Conti E (April 2003). "Structural basis of Aurora-A activation by TPX2 at the mitotic spindle". Molecular Cell. 13 (8): 691–697. doi:10.1016/s1097-2765(03)00392-7. PMID 14580337.
  6. ^ Tsuchiya Y, Byrne DP, Burgess SG, Bormann J, Bakovic J, Huang Y, Zhyvoloup A, Yu BY, Peak Chew S, Tran T, Bellany F, Tabor AB, Chan AE, Guruprasad L, Garifulin O, Filonenko V, Vonderach M, Ferries S, Eyers CE, Carroll J, Skehel M, Bayliss R, Eyers PA, Gout I (Sep 2019). "Covalent Aurora A regulation by the metabolic integrator coenzyme A". Redox Biology. doi:10.1016/j.redox.2019.101318. PMC 6812009. PMID 31546169.