AURKA
Description
The AURKA (aurora kinase A) is a protein-coding gene located on chromosome 20.
Aurora kinase A, also known as serine/threonine-protein kinase 6, is an enzyme that in humans is encoded by the AURKA gene. Aurora A is a member of a family of mitotic serine/threonine kinases. It is implicated with important processes during mitosis and meiosis whose proper function is integral for healthy cell proliferation. Aurora A is activated by one or more phosphorylations and its activity peaks during the G2 phase to M phase transition in the cell cycle.
== Discovery == The aurora kinases were first identified in 1990 during a cDNA screen of Xenopus eggs. The kinase discovered, Eg2, is now referred to as Aurora A. However, Aurora A's meiotic and mitotic significance was not recognized until 1998.
== Aurora kinase family == The human genome contains three members of the aurora kinase family: Aurora kinase A, Aurora kinase B and Aurora C kinase. The Xenopus, Drosophila, and Caenorhabditis elegans genomes, on the other hand, contain orthologues only to Aurora A and Aurora B. In all studied species, the three Aurora mitotic kinases localize to the centrosome during different phases of mitosis. The family members have highly conserved C-terminal catalytic domains. Their N-terminal domains, however, exhibit a large degree of variance in the size and sequence.
Aurora kinase A (AURKA) is a mitotic serine/threonine kinase that plays a crucial role in regulating cell cycle progression. It associates with the centrosome and spindle microtubules during mitosis, participating in essential mitotic events such as spindle formation, centrosome duplication, separation, and maturation, chromosomal alignment, the spindle assembly checkpoint, and cytokinesis. It is essential for normal spindle positioning during mitosis, and for the localization of NUMA1 and DCTN1 to the cell cortex during metaphase. It is also required for the initial activation of CDK1 at centrosomes. AURKA phosphorylates a wide range of target proteins, including ARHGEF2, BORA, BRCA1, CDC25B, DLGP5, HDAC6, KIF2A, LATS2, NDEL1, PARD3, PPP1R2, PLK1, RASSF1, TACC3, p53/TP53, and TPX2, influencing various cellular processes. AURKA regulates KIF2A tubulin depolymerase activity, contributing to microtubule formation and/or stabilization. It is essential for normal axon formation and plays a role in microtubule remodeling during neurite extension. AURKA serves as a key regulator in the p53/TP53 pathway, particularly in checkpoint-response pathways critical for preventing oncogenic transformation of cells. It phosphorylates and destabilizes p53/TP53, thereby influencing its activity. AURKA also phosphorylates its own inhibitors, the protein phosphatase type 1 (PP1) isoforms, to inhibit their activity. It inhibits cilia outgrowth and is essential for cilia disassembly through phosphorylation of HDAC6 and subsequent deacetylation of alpha-tubulin. AURKA regulates the protein levels of the anti-apoptosis protein BIRC5 by suppressing the expression of the SCF(FBXL7) E3 ubiquitin-protein ligase substrate adapter FBXL7 through phosphorylation of the transcription factor FOXP1.
AURKA is also known as AIK, ARK1, AURA, BTAK, PPP1R47, STK15, STK6, STK7.
