Rabut Group Research

The general objective of our team is to investigate at the molecular level the functions and regulatory mechanisms of protein ubiquitylation.

Ubiquitylation is an essential posttranslational protein modification conserved in all eukaryotes. It encodes complex molecular signals that control the activity and degradation of a very wide array of cellular proteins. Defects in this process lead to unbalances in the cellular protein content and are associated with numerous human pathologies, including cancers and neurodegenerative diseases.

The fundamental principles governing ubiquitylation are now understood; however we are far from knowing its full functional spectrum. For instance, many of the ubiquitylation and deubiquitylation enzymes that attach and remove ubiquitin to and from cellular proteins are not comprehensively studied and their specific substrates and functions are often described only partially, if at all. Our main objective is therefore to identify and characterize new cellular pathways regulated by ubiquitylation. To this end, we are using budding yeast (S. cerevisiae) as a model organism and a combination of genetic, biochemical, proteomics and live cell imaging approaches.

Bimolecular fluorescence complementation allows us to uncover new interactions between ubiquitylation enzymes. The picture shows the interaction between the enzymes Asi3 and Ubc7 (green), which takes place at periphery of the nucleus (red) - © Gwenaël RABUT / IGDR


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