SUMOylation is a post-translational modification, which consists in the covalent conjugation of the small protein SUMO to lysine-side chains of proteins. SUMOylation has been involved in the regulation of most cellular processes. Because of its pleiotropic roles, SUMOylation is emerging as a promising target for the treatment of cancers. In particular, G. Bossis’s team (IGMM) has shown that SUMOylation plays a critical role in Acute Myeloid Leukemias (AML) response to therapies (chemotherapies, differentiation therapies and epigenetic therapies). However, the study of SUMOylation is hampered by the lack of tools to modulate its conjugation to target proteins. To fill this gap, we are, together with M. Amblard’s team (IBMM), developing a new kind of SUMOylation inhibitors.
As SUMOylation is highly dynamic and plays critical roles in numerous cellular processes, a general inhibition of SUMOylation can have pleiotropic effects and have deleterious consequences on normal cells. Finding ways to inhibit SUMOylation in a controlled manner would thus be highly valuable both to study the function of SUMOylation and for therapeutic intervention to limit potential side effects. On the basis of peptide-based SUMOylation inhibitors we already identified, we therefore propose to develop photoinducible inhibitors of SUMOylation.
The student recruited on this interdisciplinary project will be trained for peptide synthesis and incorporation of the photo-caged amino-acids at the IBMM and will test the activity of the photo-inducible peptides in cancer cells, in particular AMLs, at the IGMM.
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