Journal
FRONTIERS IN MICROBIOLOGY
Volume 3, Issue -, Pages -Publisher
FRONTIERS MEDIA SA
DOI: 10.3389/fmicb.2012.00066
Keywords
Kaposi's sarcoma-associated herpesvirus; ubiquitin; proteasome; polyubiquitin; RING
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Funding
- Health and Labor Sciences Research Grants [H23-AIDS-Ippan-002]
- Ministry of Health, Labor and Welfare of Japan
- Ministry of Education, Culture, Sports, Science and Technology of Japan
- Takeda Science Foundation
- Japan Health Sciences Foundation
- New Energy and Industrial Technology Development Organization (NEDO) of Japan
- Grants-in-Aid for Scientific Research [21590113, 21590091] Funding Source: KAKEN
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Ubiquitination is a post-translational modification in which one or more ubiquitin molecules are covalently linked to lysine residues of target proteins. The ubiquitin system plays a key role in the regulation of protein degradation, which contributes to cell signaling, vesicular trafficking, apoptosis, and immune regulation. Bacterial and viral pathogens exploit the cellular ubiquitin system by encoding their own proteins to serve their survival and replication in infected cells. Recent studies have revealed that Kaposi's sarcoma-associated herpesvirus (KSHV) manipulates the ubiquitin system of infected cells to facilitate cell proliferation, anti-apoptosis, and evasion from immunity. This review summarizes recent developments in our understanding of the molecular mechanisms used by KSHV to interact with the cellular ubiquitin machinery.
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