E3 ubiquitin ligases in neurodegeneration, autoinflammation and cancer

E3 ubiquitin ligases in neurodegeneration, autoinflammation and cancer

Project details

E3 ubiquitin ligases are enzymes that attach the small protein ubiquitin to target proteins in a post-translational modification called ubiquitination. The human genome encodes for more than 700 ubiquitin ligases with diverse functions in the human cell. 

This project will focus one of the E3 ubiquitin ligases linked to different human diseases to understand their molecular and cellular functions. Depending on the student’s interest, this project can involve methods like structural biology, biochemistry and biophysics, or cell biology and proteomics. We are also trying to enhance the toolbox to study E3 ligases, and the project could also focus on assay development to efficiently and specifically probe E3 ligase activity in vitro and screen for small molecules modulating E3 ligase activity as drug candidates. 

About our research group

Ubiquitination is a post-translation modification, best known for directing proteins towards proteasomal degradation, but it actually regulates almost all processes inside the cell. 

The Lechtenberg lab is interested in E3 ubiquitin ligases, the enzymes that attach ubiquitin to a substrate. We aim to understand the role of E3 ligases in health and disease to ultimately find therapies against diseases including neurodegeneration, autoinflammation and cancers. 

We combine studies on the molecular (structural biology, biochemistry, biophysics) and cellular (cell biology, proteomics) levels and closely collaborate with other labs (Komander, Feltham, Dewson) to obtain a comprehensive multi-level understanding of E3 ligase biology. 

We are also involved in a multi-Institute project to exploit the ubiquitin system with novel drug technology (protein degraders or PROTACs) that specifically degrades target proteins. 


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