Ubiquitination is a post-translational modification process that controls the degradation, signalling and activity of many, if not all, cellular proteins. Ubiquitination needs to be finely tuned and is catalysed and controlled by several players: ubiquitin, the E1 ubiquitin activating enzyme, the E2 ubiquitin conjugating enzymes, the E3 ubiquitin ligases, which compose the ubiquitination cascade. Given the importance of ubiquitination in several fundamental biological pathways, this process has become with no surprise the target of search and development of pharmacological drugs.
Tripartite Motif (TRIM) proteins participate in ubiquitin and ubiquitin-like modifications and form a large family of over 70 RING-type ubiquitin E3 ligases that allow proper transfer of the ubiquitin moiety to the target. Besides the N-terminal RING domain, the TRIM proteins display one or two B-box domain(s) and a Coiled-coil region responsible for their homo- and hetero-interactions. The combination of these 3 domains, the tripartite motif, is the hallmark of this class of proteins.
TRIM proteins are involved in many diseases and clinically relevant processes emphasizing the need for deep knowledge of TRIM proteins mechanism of action in order to design and develop targeting strategies. The ultimate goal of TRIM-NET is determining how TRIM proteins contribute to disease and how we can use this information to develop novel therapeutics for TRIM family members that are involved in common and rare pathologies, thus heavily impacting on public health.
TRIESTE, Italy – February 18-19, 2019
Department of Life Sciences
University of Trieste