Aurora Kinase

Aurora kinases are highly conserved serine/threonine kinases that regulate mitotic progression and maintain chromosomal stability during cell division.[1][2] The mammalian Aurora kinase family comprises AURKA, AURKB, and AURKC, which share a conserved catalytic domain but differ in subcellular localization, substrate specificity, and mitotic function.[1][3] Mechanistically, AURKA controls centrosome maturation, spindle assembly, and G2/M transition, whereas AURKB functions as a chromosomal passenger kinase that regulates chromosome segregation and cytokinesis.[2][3][4] AURKC exhibits overlapping functions with AURKB but is predominantly associated with meiotic processes and germ-cell development.[5] Dysregulated Aurora kinase expression promotes genomic instability, aneuploidy, and uncontrolled proliferation, and overexpression of AURKA or AURKB has been reported in multiple human malignancies.[1][2][6] Therefore, Aurora kinase signaling has emerged as a central pathway linking mitotic control to tumorigenesis and therapeutic resistance.[6][7] Compared with related isoforms, AURKA has received particular attention because of its roles in spindle organization, DNA replication, and synthetic lethal interactions with tumor suppressor pathways, supporting its application as a precision oncology target.[2] For experimental applications, selective and pan-Aurora kinase inhibitors have been developed to disrupt mitotic progression, induce polyploidy or apoptosis, and evaluate Aurora-dependent vulnerabilities in cancer models.[4][7]