When a cell is infected with a virus, it defends itself by responding with the production of hundreds of proteins. A large proportion of the proteins that are made during the infection are encoded by interferon-stimulated genes. The tripartite motif (TRIM) proteins represent a family whose members fall into this category. Human genomes encode more than 80 TRIM proteins. As expected by their regulation pattern, many of these TRIM proteins enhance the innate antiviral immune response. Other identified roles for TRIM proteins include processes such as autophagy and carcinogenesis.
Most TRIM proteins act as E3 ubiquitin ligases, enzymes that attach ubiquitin and ubiquitin-like molecules onto “target” proteins, our lab is attempting to identify the targets of the TRIM proteins. Yeast two-hybrid is a classic method for detecting protein-protein interactions in an unbiased manner. We have developed a pipeline of experiments for following up on interactions detected using the yeast two-hybrid system.
For the 2017-18 academic year, my laboratory has funding from Montana INBRE for this project. Also, the INBRE funding will allow my laboratory to merge the Colorado Tick Fever virus research with the TRIM project.