“Dissecting selective protein degradation in health and disease”, Anton Khmelinskii, IMB Mainz, Germany
Speaker: Anton Khmelinskii, IMB Mainz, Germany
Host: Bachir El Debs, BioMed X
Selective protein degradation is involved in most cellular processes and contributes to proteome homeostasis through the removal of unnecessary or abnormal proteins. The ubiquitin-proteasome system (UPS) plays a key role in selective protein degradation, whereby a cascade of E1 ubiquitin-activating, E2 ubiquitin-conjugating and E3 ubiquitin-protein ligase enzymes mark proteins with polyubiquitin chains for proteasomal degradation. Deubiquitinating enzymes, which remove ubiquitin marks and replenish the pool of free ubiquitin, are involved at various stages of the targeting and degradation processes. Despite the central role of the UPS in protein degradation and its association with various diseases and ageing, many UPS components remain poorly characterized and our understanding of specificity in the UPS is inadequate. I will describe our previous work where we developed proteomic approaches to gain insights into selective protein degradation, including unbiased screening pipelines to identify substrates and functions for various components of the ubiquitin-proteasome system and to define signals involved in substrate recognition. I will introduce our ongoing work aimed at understanding how cells deal with mislocalized proteins.
• Since 2018: Group Leader, Institute of Molecular Biology (IMB), Mainz
• 2010–2017: Postdoctoral Researcher, Center for Molecular Biology (ZMBH), Heidelberg University; Donnelly Centre for Cellular and Biomolecular Research, University of Toronto; European Molecular Biology Laboratory (EMBL), Heidelberg
• 2010: PhD in Biology, University of Heidelberg
• 2005: Licenciatura degree in Biochemistry, University of Lisbon