Name: Kim Florian Taupitz
Diploma / M.Sc degree: Westfälische Wilhelms-Universität Münster, Germany
(September 2013)

PhD Project: Investigations on the interaction of the posttranslational modifier SUMO with its binding partners using new methods in protein chemistry

Abstract of Research Project

Posttranslational modifications represent one option for cells to react rapidly on external influences. They have a direct influence on the activity, stability, conformation, intracellular localization and protein-protein interaction pattern of the substrate protein. Besides the conjugation of small chemical moieties like phosphate groups, the substrate protein can also be modified by small proteins such as ubiquitin or ubiquitin-like proteins (Ubls), e.g. SUMO (small ubiquitin-related modifier). Hundreds of proteins are sumoylated in human cells. It has been shown that a misregulation of the SUMO conjugation/deconjugation cycle is related to the emergence of neurodegenerative diseases such as carcinogenesis, Alzheimer’s, Parkinson’s or Huntington’s disease.

SUMO can interact non-covalently with proteins that possess a SIM (SUMO-interacting motif) and thereby effect new protein-protein interactions. However, due to the relatively weak SIM-SUMO interaction, the precise role of sumoylation if often difficult to study.

In my thesis I want to further investigate the SIM-SUMO interaction using new methods in protein chemistry. Chemical crosslinkers will be explored to stabilize the protein complexes for further investigation.