Post translational modifications (PTMs) are orchestrated by highly active and reversible enzymatic systems to regulate the functional diversity of proteins. Because of their dynamic nature, PTMs are used by the cell as a controllable system to regulate a wide variety of processes. Studying modifications of proteins will give us more insight in how the cell uses PTMs to regulate cellular processes and how different PTMs act together to adjust the function of proteins. The research described in this thesis focuses one of these PTMs, the Small ubiquitin-Like Modifier (SUMO). SUMOs are proteins that are covalently attached to lysines in target proteins. These studies have uncovered hundreds of SUMO target proteins and acceptor sites and revealed a role for SUMOylation in protein degradation, cell cycle progression and DNA repairLUMC / Geneeskund
