Aurora kinase B (AURKB, also known as Aurora 1) is a serine/threonine-protein kinase component of the chromosomal passenger complex (CPC), a complex that acts as a key regulator of mitosis []. AURKB has various mitotic functions, including chromosome-microtubule interactions, sister chromatid cohesion, the spindle-assembly checkpoint and cytokinesis [, , ]. It phosphorylates chromatin proteins such as histone H3 to aid in mitotic chromosome condensation and contributes to the spindlecheckpoint []. Its expression is cell cycle-regulated, with a low in G1/S, an increase during G2 and M [].The Aurora kinases are highly conserved serine/threonine kinases that regulate chromosomal alignment and segregation during mitosis and meiosis. Three mammalian Aurora kinases, Aurora A, B and C, have been identified. 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 domain share little sequence identity and confer unique protein-protein interaction abilities among the Aurora kinases []. They are differentially expressed at high levels in rapidly dividing tissues such as hematopoietic cells (A and B) and germ cells (C only). Their expression is low or absent in most adult tissues due to their lower rates of proliferation [].
Inner centromere protein (INCENP) is a component of the chromosomal passenger complex (CPC), which is an important regulator of mitosis. CPC ensures correct alignment and segregation of chromosomes at the centromere. INCENT interacts with several other CPC subunits [, , ]and it activates subunits AURKB and AURKC []; it also interacts with the tubulin beta chain []. Two paralogues exist in Xenopus named INCEP A and B.
Aurora kinase C (AURKC) is a serine/threonine-protein kinase found in some mammals. It is a component of the chromosomal passenger protein that forms complexes with Aurora-B and inner centromere protein (INCENP), and it has redundant cellular functions with AURKB []. It is required for spermatogenesis and oocyte development [, ]. The overexpression of AURKC has been linked to various cancers []. Overexpression of Aurora-C displaces the centromeric localisation of chromosomal passenger complex (CPC) proteins, including Aurora-B []. CPC plays a crucial role in controlling accurate chromosome segregation and cytokinesis during cell division.The Aurora kinases are highly conserved serine/threonine kinases that regulate chromosomal alignment and segregation during mitosis and meiosis. Three mammalian Aurora kinases, Aurora A, B and C, have been identified. 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 domain share little sequence identity and confer unique protein-protein interaction abilities among the Aurora kinases []. They are differentially expressed at high levels in rapidly dividing tissues such as hematopoietic cells (A and B) and germ cells (C only). Their expression is low or absent in most adult tissues due to their lower rates of proliferation [].
