InterPro domain: IPR030616

Aurora kinase was discovered by Glover and colleagues in a screen for genes required to maintain the centrosome cycle in Drosophila [ 1 ]. Its yeast homologue Ipl1 (also known as spindle assembly checkpoint kinase) was found to regulate chromosome segregation [ 2 ]. Subsequently, three mammal Aurora kinases, Aurora A, B and C, have been identified.

They are highly conserved serine/threonine kinases that regulate chromosomal alignment and segregation during mitosis and meiosis [ 3 ]. They all contain a protein kinase domain and a destruction box (D-box) recognised by the multi-subunit E3-ubiquitin ligase anaphase promoting complex/cyclosome (APC/C), which mediates their proteasomal degradation. However, their N-terminal domains share little sequence identity and confer unique protein-protein interaction abilities among the Aurora kinases [ 4 ].

Functionally, Aurora A associates with centrosome, while Aurora B and Aurora C are parts of the chromosome passenger complex (CPC) [ 5 , 5 ]. Aurora C plays a role in the meiotic cell cycle, but does not seem to be essential for cell divisions in somatic cells [ 6 ].

This entry also includes a number of uncharacterised proteins, predominantly from bacteria.

1. Mutations in aurora prevent centrosome separation leading to the formation of monopolar spindles. Cell 81, 95-105
2. Type 1 protein phosphatase acts in opposition to IpL1 protein kinase in regulating yeast chromosome segregation. Mol. Cell. Biol. 14, 4731-40
3. Aurora at the pole and equator: overlapping functions of Aurora kinases in the mitotic spindle. Open Biol 3, 120185
4. The cellular geography of aurora kinases. Nat. Rev. Mol. Cell Biol. 4, 842-54
5. Direct association with inner centromere protein (INCENP) activates the novel chromosomal passenger protein, Aurora-C. J. Biol. Chem. 279, 47201-11