Inactivation of the CYLD Deubiquitinase by HPV E6 Mediates Hypoxia-Induced NF-κB Activation
摘要：
Summary The biochemical mechanisms that underlie hypoxia-induced NF-κB activity have remained largely undefined. Here, we find that prolonged hypoxia-induced NF-κB activation is restricted to cancer cell lines infected with high-risk human papillomavirus (HPV) serotypes. The HPV-encoded E6 protein is necessary and sufficient for prolonged hypoxia-induced NF-κB activation in these systems. The molecular target of E6 in the NF-κB pathway is the CYLD lysine 63 (K63) deubiquitinase, a negative regulator of the NF-κB pathway. Specifically, hypoxia stimulates E6-mediated ubiquitination and proteasomal degradation of CYLD. Given the established role of NF-κB in human carcinogenesis, these findings provide a potential molecular/viral link between hypoxia and the adverse clinical outcomes observed in HPV-associated malignancies.
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DOI：
10.1016/j.ccr.2008.10.007
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年份：
2008
Elsevier
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掌桥科研
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