Abstract
Viruses alter specific host cell targets to counteract possible defense mechanisms aimed at eliminating infectivity and viral propagation. The SUMO conjugating enzyme Ubc9 functions as a hub for protein sumoylation, whilst also providing an interactive surface for sumoylated proteins through noncovalent interactions. The targeting of Ubc9 by viruses and viral proteins is thus highly beneficial for the disruption of both protein modification and protein-protein interaction mechanisms with which proteins increase their functional repertoire in cells. This review explores some of the clever mechanisms adopted by viruses to deregulate Ubc9, influence effector pathways and positively impact viral persistence consequently.
Original language | English (US) |
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Pages (from-to) | 27-33 |
Number of pages | 7 |
Journal | IUBMB Life |
Volume | 66 |
Issue number | 1 |
DOIs | |
State | Published - Jan 2014 |
Externally published | Yes |
Keywords
- SUMO
- SUMO UBC9 enzyme
- viral proteins
ASJC Scopus subject areas
- Biochemistry
- Molecular Biology
- Genetics
- Clinical Biochemistry
- Cell Biology