The tumor suppressor p27kip1 is regulated at post-translational level and its deregulation in human cancer is mainly due to its accelerated proteasomal degradation. Our results demostrate that the presence of threonine in position 198 is of primary importance for the regulation of the protein stability and for the control of cell motility and that p27 functions are also affected by SUMOylation. This thesis work provides new insight into p27 regulation by both conformational changes in its unstructured c-terminal domain and post-translational modifications
