Journal
BIOLOGY OF THE CELL
Volume 104, Issue 3, Pages 121-138Publisher
WILEY
DOI: 10.1111/boc.201100105
Keywords
Post-translational modification; Proteasomes/ubiquitin; Proteinsorting/trafficking/targeting; Viruses
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Funding
- Pacific Southwest Regional Center of Excellence for Biodefense and Emerging Infectious Diseases [U54 AI065359]
- National Institutes of Health [R01 AI069317]
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Nucleocytoplasmic trafficking of many cellular proteins is regulated by nuclear import/export signals as well as post-translational modifications such as covalent conjugation of ubiquitin and small ubiquitin-related modifiers (SUMOs). Ubiquitination and SUMOylation are rapid and reversible ways to modulate the intracellular localisation and function of substrate proteins. These pathways have been co-opted by some viruses, which depend on the host cell machinery to transport their proteins in and out of the nucleus. In this review, we will summarise our current knowledge on the ubiquitin/SUMO-regulated nuclear/subnuclear trafficking of cellular proteins and describe examples of viral exploitation of these pathways.
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