Herzmuskelzellen der Ratte

Sommer Lab

Intracellular Proteolysis


Research in the Sommer lab focuses on the dissection of the molecular machinery involved in protein-ubiqui-tylation and the cellular processes controlled by it.

Covalent attachment of ubiquitin onto proteins rapidly changes the attributes of the client, such as its half-life, conformation, subcellular localization or its interaction with partner proteins. In eukaryotic cells ubiquitylation serves to regulate essential cellular activities, such as the progression in cell cycle, endocytosis, autophagy, and maintenance of protein homeostasis. Consequently, defects in the ubiquitylation machinery are associated with the development of severe malignancies like cancer, neurodegeneration and cardivascular diseases. Therefore, the characterization of the function and regulation of ubiquitylating enzymes is of general importance for the understanding of fundamental cell-biological processes and will contribute to identify specific entry points for therapeutical intervention.



In our group we employ genetic, cell-biological, biochemical and microscopic techniques to analyze the composition and function of selected ubiquitin ligases as well as their physiological role in the cell. We also use purified proteins in in vitro assays to study the mechanistic details on how individual ubiquitin conjugating enzymes generate appointed ubiquitin signals.




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