Aurora kinases (AURKs) are a member of the serine/threonine kinase family, whose activation is essential for cell division processes by controlling mitosis. Aurora A kinase (AURKA) regulates centrosome maturation, mitotic entry, bipolar spindle formation and function, as well as cytokinesis. Aurora B (AURKB) is a mitotic checkpoint kinase in the cell cycle, ensuring correct chromosome segregation and normal progression through mitosis. Previous studies have suggested that AURKs are overexpressed in many cancers arising from breast, colon, ovary, and other cancers, which affects aberrant cell cycle regulation, resistance to cell death and metastasis. In addition, the activation and degradation of AURKs are regulated by ubiquitination. Ubiquitin-specific peptidase 37 (USP37), known as a deubiquitinating enzyme, prevents protein degradation through enzymatic activity which shows detachment of ubiquitin from the targeted protein, resulting in the control of protein stabilization. Here, we reveal the interaction between AURKs and USP37, and it associated with the regulation of cells which may have a significant role in the development of therapeutic agents for cancer.