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Description

Aurora kinase B (UniProt: Q96GD4, also known as EC:2.7.11.1, Aurora 1, Aurora- and IPL1-like midbody-associated protein 1, AIM-1, Aurora/IPL1-related kinase 2, ARK-2, Aurora-related kinase 2, STK-1, Serine/threonine-protein kinase 12, Serine/threonine-protein kinase 5, Serine/threonine-protein kinase aurora-B) is encoded by the AURKB (also known as AIK2, AIM1, AIRK2, ARK2, STK1, STK12, STK5) gene (Gene ID: 9212) in human. Aurora Kinase B is a serine/threonine-protein kinase component of the chromosomal passenger complex (CPC), a complex that acts as a key regulator of mitosis. It is a key component of the cytokinesis checkpoint, a process required to delay abscission to prevent both premature resolution of intercellular chromosome bridges and accumulation of DNA damage. The CPC complex has essential functions at the centromere in ensuring correct chromosome alignment and segregation and is required for chromatin-induced microtubule stabilization and spindle assembly. Aurora kinase B phosphorylates the CPC complex subunits BIRC5/survivin, CDCA8/borealin and INCENP and phosphorylation of INCENP leads to increased Aurora kinase B activity. Five isoforms of Aurora Kinase are reported that are produced by alternative splicing. Its expression is shown to be cell-cycle regulated, with low expression in G1/S phase and an increase during G2 and M phase. Following M phase its expression declines. Cancer cells display high expression of Aurora kinase B during M phase. Disruption in regulation of Aurora kinase B causes perturbation of chromosomal integrity in cancer cells through its dominant-negative effect on cytokinesis. High level expression is observed in the thymus. It is also expressed in the spleen, lung, testis, colon, placenta and fetal liver. Substitution of Lysine 106 with arginine leads to loss of its kinase activity and severely impairs mitotic progression.