Title: Function and dynamics of protein N-terminal modifications in health and disease. Spotlight on NatB-dependent acetylation and its role in apoptosis.
N-terminal protein modifications (NPMs) are among the first and fastest responses to the cellular environment, influencing not only the modified protein but also cell, tissue, and whole organism phenotypes. One major NPM is N-terminal (Nt-) acetylation, an essential multitasking protein modification implicated in many diseases. The characterization of proteins subjected to NPM and of the enzymes involved requires the setting of specific approaches, particularly at the level of proteomics. During my seminar, I will give you an overview of the approaches we have developed in our group that have helped us to characterize the most important NPMs in many different organisms and ultimately to design specific inhibitors for some of the enzymes involved. Finally, I will present one of our unpublished works, focusing on the elucidation of the molecular mechanisms linking N-terminal acetyltransferase B (NatB), one of the major N-acetyl transferases, to apoptosis and its relationship with protein homeostasis.
Friday, March 17th 2023, at 16.00 Central European Time
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Carmela Giglione is an Italian biochemist who has made fundamental contributions in the field of protein modifications. She leads her group at the Institute for Integrative Biology of the Cell (I2BC), Université Paris Saclay, CEA, CNRS. Her major interests are essential widespread modifications affecting the N-termini of proteins, which are mainly but not only cotranslationals. In this context, she has characterized these modifications in many different organisms including parasites, and rationally designed specific potent inhibitors for the enzymes involved in these modifications. She has also developed several bioinformatics tools to disseminate data concerning these modifications. Currently she seeks to understand the nature and the biological effect of these modifications, in particular at the level of the cell partition in sub-compartments defined or not by membranes, and the impact of these modifications on the maintenance of a functional proteome. Giglione is co-founder and elected member of the managing board of the International Society of Protein Termini.