Molecular Cell Biology
Head: Dr. Anja Bremm
Protein ubiquitination emerged as a fundamental regulatory process in the cell, and both proteolytic and non-proteolytic functions have been attributed to this small protein modifier. The various cellular responses to ubiquitin signals are highly regulated by factors that recognize or remove the modification (Ubiquitin-binding domain (UBD)-containing proteins and deubiquitinating enzymes (DUBs), respectively). Ubiquitin is attached to substrate lysine residues and can assemble at least eight differently linked polymers. Importantly, these ubiquitin chains have been associated with distinct cellular outputs, further increasing the astonishing complexity in the ubiquitin system.
Our lab investigates the role of protein ubiquitination in adaptive responses to cellular stress, e.g. hypoxia, oxidative damage or starvation. In this context, we are particularly interested in the function and regulation of DUBs. Altered DUB activity is associated with a multitude of pathologies including cancer and Alzheimer’s diseases. Therefore, DUBs represent promising novel structures for targeted therapy. We aim to increase our understanding of the physiological functions and control mechanisms of these important and versatile enzymes.
Figure 1: Schematic overview of the ubiquitin system. DUBs play essential roles in the correct outcome of the ubiquitin code.