Deubiquitination in virus infection.
Post-translational modification of proteins and peptides by ubiquitin, a highly evolutionarily conserved 76 residue protein, and ubiquitin-like modifiers has emerged as a major regulatory mechanism in various cellular activities. Eukaryotic viruses are known to modulate protein ubiquitination to their advantage in various ways. At the same time, the evidence for the importance of deubiquitination as a viral target also is growing. This review centers on known viral interactions with protein deubiquitination, on viral enzymes for which deubiquitinating activities were recently demonstrated, and on the roles of viral ubiquitin-like sequences.
Lindner
Holger A
HA
Biotechnology Research Institute, National Research Council of Canada, 6100 Avenue Royalmount, Montreal, Quebec, Canada H4P 2R2. Holger.Lindner@cnrc-nrc.gc.ca
D004798:Enzymes / Q000378:metabolism; D005057:Eukaryotic Cells / Q000378:metabolism / Q000821:virology; D011499:Protein Processing, Post-Translational; D014452:Ubiquitins / Q000378:metabolism*; D014764:Viral Proteins / Q000378:metabolism*; D014780:Viruses / Q000201:enzymology / Q000378:metabolism*
D004798:Enzymes; D014452:Ubiquitins; D014764:Viral Proteins