Research Topic

Exploitation of host ubiquitination by pathogens

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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 ...

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


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