Structure and function of E3 ubiquitin ligases

Structure and function of E3 ubiquitin ligases

Project details

E3 ubiquitin ligases catalyse the covalent addition of the small protein ubiquitin to other proteins in a process called ubiquitination. Ubiquitination is a post-translational modification that regulates almost all processes inside the cell.

This project aims to understand the structure and function of members of the RING-between-RING (RBR) family of E3 ubiquitin ligases and their roles in diseases such as inflammation and cancer with the ultimate goal to find new treatment options.

The project builds on our previous studies on the E3 ubiquitin ligase HOIP (Lechtenberg, Nature 2016 529(7587):546) and is suitable for a student interested in learning a diverse set of techniques including recombinant protein expression and purification, biochemical assays, structural biology (X-ray crystallography) as well as basic cell biological and proteomic methods.

About our research group

The Lechtenberg group started in the new Ubiquitin Signalling division in March 2019. Our lab utilises a multi-disciplinary approach to investigate novel, understudied E3 ubiquitin ligases with a particular interest in the family of RING-between-RING (RBR) E3 ligases.

We aim to comprehensively study these E3 ligases from the molecular details of their catalytic mechanism and their regulation all the way to their functions in their larger signalling pathways in the human cell by combining structural biology, biochemical, biophysical, and cell biological methods.

Our ultimate goal is to link fundamental biological insights with a translational approach to develop novel drug candidates and treatment options in various diseases, with an initial focus on cancer and autoimmune diseases.


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