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Open Access Gold as soon as Publ. Version/Full Text is submitted to ZB.
Viral mimicry to usurp ubiquitin and sumo host pathways.
Viruses 7, 4854-4877 (2015)
Posttranslational modifications (PTMs) of proteins include enzymatic changes by covalent addition of cellular regulatory determinants such as ubiquitin (Ub) and small ubiquitin-like modifier (SUMO) moieties. These modifications are widely used by eukaryotic cells to control the functional repertoire of proteins. Over the last decade, it became apparent that the repertoire of ubiquitiylation and SUMOylation regulating various biological functions is not restricted to eukaryotic cells, but is also a feature of human virus families, used to extensively exploit complex host-cell networks and homeostasis. Intriguingly, besides binding to host SUMO/Ub control proteins and interfering with the respective enzymatic cascade, many viral proteins mimic key regulatory factors to usurp this host machinery and promote efficient viral outcomes. Advanced detection methods and functional studies of ubiquitiylation and SUMOylation during virus-host interplay have revealed that human viruses have evolved a large arsenal of strategies to exploit these specific PTM processes. In this review, we highlight the known viral analogs orchestrating ubiquitin and SUMO conjugation events to subvert and utilize basic enzymatic pathways.
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Publication type
Article: Journal article
Document type
Review
Keywords
Analogue ; Dub ; Mimicry ; Senp ; Sumo ; Ubiquitin ; Virus
ISSN (print) / ISBN
1999-4915
e-ISSN
1999-4915
Journal
Viruses
Quellenangaben
Volume: 7,
Issue: 9,
Pages: 4854-4877
Publisher
MDPI
Non-patent literature
Publications
Reviewing status
Peer reviewed
Institute(s)
Institute of Virology (VIRO)