In cellular environment protein abundance and half-life are determined by ubiquitin-proteasomal system. Ubiquitin ligases recognize a highly specific peptide motif (degron) and transfer polyubiquitin chains to their respective substrates that eventually lead to degradation of the target protein by proteasome. Ubiquitin ligases are often inactive and their activation comes from external stimuli. Currently we are identifying crucial proteins in blood forming stem cells that are regulated by ubiquitin signaling. Since each ubiquitin ligase can recognize its target proteins through a specific degron, we are interested in delineating ubiquitin ligase-target protein interactions that are triggered by differentiation stimulus in stem cells. This will provide key insights on how ubiquitin signaling plays a vital role in stem cell differentiation and how perturbations in these networks can lead to disorders such as cancer.
Contact: Agatheeswaran Subramaniam, agatheeswaran.subramaniam@med.lu.se