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- Stabilization of E2-EPF UCP protein is implicated in hepatitis B virus-associated hepatocellular carcinoma progression
- Jung Hwa Lim; D G Kim; Dae Yeul Yu; Hyun Mi Kang; Kyung Hee Noh; Dae Soo Kim; Dongmin Park; Tae Kyung Chang; Dong-Soo Im; Jung Cho Rok
- Bibliographic Citation
- Cellular and Molecular Life Sciences, vol. 76, no. 13, pp. 2647-2662
- Publication Year
- Hepatitis B virus (HBV) X protein (HBx) is associated with hepatocarcinogenesis. E2-EPF ubiquitin carrier protein (UCP)
catalyzes ubiquitination of itself and von Hippel？Lindau protein (pVHL) for degradation and associates with tumor growth
and metastasis. However, it remains unknown whether HBx modulates the enzyme activity of UCP and thereby influences
hepatocarcinogenesis. Here, we show that UCP is highly expressed in liver tissues of HBx-transgenic mice, but not nontransgenic
mice. UCP was more frequently expressed in HBV-positive liver cancers than in HBV-negative liver cancers.
HBx binds to UCP specifically and serotype independently, and forms a ternary complex with UCP and pVHL. HBx inhibits
self-ubiquitination of UCP, but enhances UCP-mediated pVHL ubiquitination, resulting in stabilization of hypoxia-inducible
factor-1α and -2α. HBx and UCP stabilize each other by mutually inhibiting their ubiquitination. HBx promotes cellular
proliferation and metastasis via UCP. Our findings suggest that UCP plays a key role in HBV-related hepatocarcinogenesis.
- HBxTumor progressionpVHLHIFUbiquitination
- Appears in Collections:
- Division of Research on National Challenges > Stem Cell Convergenece Research Center > 1. Journal Articles
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