Phosphorylation by aurora kinase A induces Mdm2-mediated destabilization and inhibition of p53

By H. Katayama, Kaori Sasai, H. Kawai, Zhi-Min Yuan, J. Bondaruk, F. Suzuki, S. Fujii, R. Arlinghaus, B. Czerniak, S. Sen. Nature Genetics, 2004

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Pathways of apoptotic and non-apoptotic death in tumour cells (2004, background): “So, amplification of the aurora-A gene might result in its overexpression, which would lead to increased degradation of p53 and facilitate oncogenic transformatio”
Aurora-A — A guardian of poles (2005, background): “fcgi?db=gene&cmd=Retrieve&dopt=Graphics&list_uids=4193">MDM2 -mediated degradation of p53 in cancer cell line”
Cellular processing of platinum anticancer drugs (2005, background): “Silencing of aurora kinase A results in less phosphorylation of p53 at Ser315, greater stability of p53 and cell-cycle arrest at the G2–M transition, and, ultimately, increased sensitivity to cisplatin treatmen”
Aurora-kinase inhibitors as anticancer agents (2004, background): “Furthermore, a recent report shows that Aurora-A kinase activity can downregulate p53 levels, which could further contribute to genomic instability and transformation by abrogating the ability of the cell to respond to DNA damage or other insult”
Integrative genomic and proteomic analysis of prostate cancer reveals signatures of metastatic progression. (2005, background): “, 2003), and inhibit p53 (Katayama et al., 2004), among other functions.”
Roles of Aurora Kinases in Mitosis and Tumorigenesis (2007, background): “Phosphorylation of Ser(315) will enhance the affinity of p53 with Mdm2, which promotes ubiquitination and degradation of the p53 protein (95).”