Structural aspects of recently discovered viral deubiquitinating activities.
Protein ubiquitination has been identified as a regulatory mechanism in key cellular activities, and deubiquitination is recognized as an important step in processes governed by ubiquitin and ubiquitin-like modifiers. Viruses are known to target ubiquitin and ubiquitin-like modifier pathways using various strategies, including the recruitment of host deubiquitinating enzymes. Deubiquitinating activities have recently been described for proteins from three different virus families (adenovirus, coronavirus and herpesvirus), and predicted for others. This review centers on structural-functional aspects that characterize the confirmed viral deubiquitinating enzymes, and their relationships to established families of cellular deubiquitinating enzymes.
Sulea
Traian
T
Biotechnology Research Institute, National Research Council of Canada, Montréal, Québec H4P 2R2, Canada. traian.sulea@cnrc-nrc.gc.ca
Lindner
Holger A
HA
Ménard
Robert
R
D000595:Amino Acid Sequence; D008969:Molecular Sequence Data; D011487:Protein Conformation; D017386:Sequence Homology, Amino Acid; D025801:Ubiquitin / Q000378:metabolism*; D014764:Viral Proteins / Q000737:chemistry / Q000378:metabolism*; D014780:Viruses / Q000378:metabolism*
D025801:Ubiquitin; D014764:Viral Proteins