http://www.zmbh.uni-heidelberg.de/melchior/default.shtml
SUMOylation is one of the most important regulatory protein modifications in eukaryotic cells, as it controls the fate and function of hundreds of proteins in all eukaryotic cells. Reversible modification of proteins seems to be accomplished by a relatively small number of modifying enzymes and SUMO specific isopeptidases. How target specificity is achieved is thus one of the most interesting questions in the field. The overarching aim of our group is to understand mechanisms, consequences and regulation of the SUMO pathway. Current projects focus on specific SUMO enzymes and address, e.g., the functions of the RanBP2 SUMO E3 ligase complex in interphase and mitosis, the role of the essential SUMO isopeptidase USPL1, and regulation of the SUMO E1 and E2 enzymes in oxidative stress. Specific projects, which will be developed together with prospective candidate, require an intrinsic interest in molecular mechanisms and involve protein biochemistry, in vitro assays as well as mammalian cell biology.
Flotho, F. and Melchior, F. (2013) SUMOylation - a regulatory protein modification in health and disease. Annu. Rev. Biochem. 82, 357-385.
back to main