will take place on Tuesday, March 4th, 2025 from 16:00 to 17:00 hours in the CBBM Building, Ground Floor, Seminar Room Levi-Montalcini.
Host: Prof. Markus Schwaninger, Institute of Experimental and Clinical Pharmacology and Toxicology
Abstract: Ubiquitylation is a multifaceted post-translational modification that regulates a variety of cellular processes. Its complexity is based on several variables, such as the number of ubiquitin molecules attached to substrates, the type of inter-ubiquitin linkage, the formation of homo- and heterotypic chains, and the post-translational modification of ubiquitin itself. We are particularly interested in M1-linked or linear ubiquitylation, which has been studied primarily in the context of immune signaling. Our previous work has shown that the abundance of linear ubiquitin chains is regulated by several genes associated with neurodegenerative diseases. These studies revealed a previously unknown function of linear ubiquitylation in protein quality control. Linear ubiquitin chains, together with their interacting protein NEMO, remodel the interface of protein aggregates and thereby promote the local concentration of autophagy receptors, such as p62, for efficient autophagic degradation.
