Aurora kinase A (AURKA), belonging to the serine/threonine kinase family, is essential for cell division as its activation regulates mitosis. It is significantly overexpressed in multiple cancer tissues compared to normal control tissues according to the TCGA database. AURKA-mediated phosphorylation can regulate the functions of its substrates, some of which are mitosis regulators, tumor suppressors, or oncogenes. Enrichment analysis of AURKA-interacting proteins shows their involvement in classic oncogenic pathways [1].

In Ewing's sarcoma, AURKA is prominently upregulated, and its high expression is associated with shorter overall and event-free survival. Inhibition of AURKA markedly induces apoptosis and ferroptosis of Ewing's sarcoma cells and attenuates tumorigenesis in vivo, potentially through the NPM1/YAP1 axis [2].

In meningioma, AURKA is upregulated in high-grade tumors, enhancing malignant characteristics and suppressing erastin-induced ferroptosis by phosphorylating KEAP1 to activate NRF2. Suppressing AURKA combined with erastin improves the prognosis of a murine meningioma model [3].

In non-small cell lung cancer, KEAP1-deficient cells are highly sensitive to AURKA inhibition, as AURKA regulates amino acid synthesis, specifically asparagine synthesis [4].

In CREBBP-deficient B-cell malignancies, targeting AURKA induces synthetic lethality by suppressing MYC transcription and translation, delaying tumor progression in vivo [5].

In conclusion, AURKA is crucial for cell division and plays significant roles in multiple cancer types. Through gene-knockout or conditional-knockout mouse models and other in-vivo studies, we have gained insights into how AURKA contributes to tumorigenesis, such as promoting cell survival, regulating ferroptosis, and affecting amino acid metabolism and MYC-related pathways in specific cancer contexts. These findings suggest AURKA as a potential target for cancer therapy.