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Neurodegenerative diseases and Fanconi anemia

Project description

My research program concerns the structure-function study of post-translational modifications of proteins and, more specifically, the study of SUMOylation of proteins. This type of modification, ubiquitous in eukaryotes, regulates localization, function, protein stability and protein-protein interactions. As a result, SUMOylation is involved in multiple biochemical processes and plays a role in several human pathologies such as certain cancers or certain neurodegenerative diseases. Many proteins are thus SUMOylated in humans due to the sequential action of an activation enzyme E1, a conjugation E2 enzyme and an E3 ligase that brings substrate and E2 activated within a single protein complex to facilitate the transfer of SUMO from the active site of E2 to the substrate. Although most SUMO E3 ligases belong to the RING domain family of proteins, my post-doctoral studies have contributed to the structural and mechanistic characterization of smaller E3 ligases collectively referred to as “atypical SUMO E3 ligases”. A SUMO E3 ligase activity has also been proposed for several other proteins, but the molecular bases of this activity remain very often elutrive, which limits the possibilities of manipulation, particularly for therapeutic purposes. I am now planning to develop a new line of research aimed at understanding the SUMO E3 ligase activity of these proteins at the molecular level.

Laboratory

Laboratory of Pr Laurent Cappadocia (UQAM)
Laureate: Teaching allowance 2019 and 2020

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