In this thesis we investigated the molecular mechanism of a subset of USPs (Ubiquitin-Specific Proteases), a class of deubiquitinating enzymes. Our findings describe how USP7, one of the subset members, can get activated by its biological target, sketching a role for its biological partner proteins. Furthermore, we describe on a molecular level how the domain structure of USP7, but also the paralogue USP40, aids in the intrinsic activity by activating the enzyme. We show that this self-activation is a conserved mechanism, yielding valuable information for the development of inhibitory molecules, but altogether also providing insight into the biological workings and role of these USP enzymes.

, , , , , , , ,
T.K. Sixma (Titia) , A. Perrakis (Anastassis)
Erasmus University Rotterdam
hdl.handle.net/1765/115598
Erasmus MC Cancer Institute

Kim, R. (2019, March 8). Structural and Mechanistic Studies on Deubiquitinating Enzymes USP7 and USP40. Retrieved from http://hdl.handle.net/1765/115598