Konstantin Sparrer, a post doc in Michaela Gack's Lab, was the presenter at this week's Research Forum. Here is a summary of his presentation:
Tripartite motif (TRIM) proteins are known to be important modulators of signaling pathways involved in innate immunity. Structurally they consist of a RING domain with E3 ligase activity, followed by one or two BBoxes, a coiled-coil domain, and a unique C-terminal domain, which often mediates protein-protein interactions. The function of TRIM proteins is usually dependent on the ubiquitin E3 ligase activity of their RING domain, ranging from earmarking their respective targets for proteasomal degradation, or modulating the functional activity of the substrate protein through non-degradative polyubiquitination. While the role of TRIM proteins in the type-I interferon induction pathway is well characterized, their influence on other pathways of the immune system is less well established. Increasing evidence shows that type-I interferon induction and autophagy induction are tightly linked; however, the molecular mechanisms and host factors that dually regulate IFN responses and autophagy are largely unknown. Thus, we are currently studying the role of TRIM proteins in viral-induced autophagy.