Ubiquitin Family Proteins,
DNA Transactions, Chromatin Biology, Autophagy
The JENTSCH Lab
Our laboratory has a long-standing interest in proteins of the ubiquitin family. Covalent modification of proteins by attachment of ubiquitin (ubiquitylation) is best known for its function to label proteins for degradation by the proteasome. However, ubiquitylation plays non-proteolytic roles as well, e.g. for DNA repair, protein sorting, gene expression and signal transduction. Other members of the ubiquitin family, e.g. SUMO, Rub1(NEDD8), Urm1, Hub1, and Atg8, regulate the ubiquitin pathway, affect protein-protein interactions, control DNA repair, transcription, pre-mRNA splicing, or mediate autophagy.
We are conducting basic research with a focus on functional aspects related to ubiquitin family proteins. We identify the components of these systems and study their roles in vitro and in vivo. We are particularly interested in the non-proteolitic (non-proteasomal) functions of ubiquitin family proteins and currently focus primarily on their roles in DNA repair, pre-mRNA splicing and autophagy. Moreover, we have a general interest in DNA repair, genome stability and chromatin biology - in particular if ubiquitin family proteins are involved. For the "discovery phase" we primarily use the genetically tractable budding yeast (Saccharomyces cerevisiae) as a model system. However, to extend the significance of our findings made in yeast to a more universal level, we complement our studies by analyzing the respective functions also in mammalian cells. [Header illustration: structures of ubiquitin, Rub1, SUMO, Hub1]
Examples of our work with the respective papers are found here.
STEFAN JENTSCH - Director and Group Leader