The Aurora-A serine/threonine kinase is an important regulator of cell division that acts in spindle assembly and function, and is often overexpressed in tumour cells. It is most abundant during the G2 and M phases of the cell cycle, and is downregulated through APC/C–Cdh1-dependent proteosome-regulated proteolysis at the end of mitosis. The microtubule-binding protein TPX2 controls both the activity and the localisation of Aurora-A, but now Giulia Guarguaglini and colleagues (p.113) report that TPX2 also regulates the stability of Aurora-A in human cells. The authors show that RNAi silencing of TPX2 decreases Aurora-A levels in G2 and prometaphase cells, whereas overexpression of the Aurora-A-binding region of TPX2 impairs the degradation of Aurora-A in telophase cells. Moreover, Aurora-A degradation in TPX2-silenced cells requires proteosome activity, and the reintroduction of full-length TPX2 or the Aurora-A-binding region of TPX2 restores Aurora-A levels in TPX2-silenced prometaphase cells. Together, these findings reveal a new role for TPX2 in protecting Aurora-A from degradation, underscore the importance of the regulated stability of Aurora-A in mitotic control, and provide new insights into the origin of Aurora-A deregulation in tumour cells.