Ubiquitin is a posttranslational modifier. One or more ubiquitin molecules are covalently linked to the lysine residues of target proteins by an enzymatic reaction known as Ubiquitination. The substrate ubiquitination can lead to its degradation by the Ubiquitin-proteasome pathway. The pathway governs various eukaryotic cellular processes, including the cell-cycle, vesicle trafficking, antigen presentation, and signal transduction. Alternate functions of Ubiquitination are innate immune repose and trafficking. Not surprisingly, Ubiquitin signaling is a common target of viruses and bacterial pathogens, which exploit the signaling to gain entry in the host and create an environment conducive to their survival/replication inside host cells. We will present recent results that reveal the molecular mechanisms underlying the hijack of Ubiquitin signal by pathogens.

Keywords: Virus, Bacteria, Cell signaling, Structural Biology, NMR