About this Research Topic
Ubiquitination is a post-translational modification in which one or more 76 amino acid polypeptide ubiquitin molecules are covalently linked to the lysine residues of target proteins. Ubiquitinated proteins are either rapidly degraded by the 26S proteasome or targeted to various specific cellular compartments largely determined by which lysine residues within the ubiquitin molecule are used for the modification. Ubiquitination is the main pathway for protein degradation that governs a variety of eukaryotic cellular processes, including the cell cycle, vesicle trafficking, antigen presentation and signal transduction. Initially, viruses were known to modulate the host antigen presentation and immune responses by modulating the ubiquitination system. Recent studies have revealed that bacterial pathogens also exploit the host ubiquitination pathways to gain entry and to aid their survival/replication inside host cells. This Research Topic will cover recent development in understanding the biochemical and structural mechanisms on how bacterial and viral pathogens interact with the host ubiquitination pathways. We are soliciting additional manuscripts, research or review articles on this topic.
Abstract submission deadline: March 1, 2011
Full article submission deadline: May 1, 2011
Important Note: All contributions to this Research Topic must be within the scope of the section and journal to which they are submitted, as defined in their mission statements. Frontiers reserves the right to guide an out-of-scope manuscript to a more suitable section or journal at any stage of peer review.