The carboxy-terminus of the hepatitis B virus X protein is necessary and sufficient for the activation of hypoxia-inducible factor-alpha
- Authors
- Yoo, YG; Cho, S; Park, S; Lee, MO
- Issue Date
- Nov-2004
- Publisher
- ELSEVIER SCIENCE BV
- Keywords
- hepatitis B virus X protein; hypoxia-inducible factor-1 alpha; hepatitis B virus
- Citation
- FEBS LETTERS, v.577, no.1-2, pp 121 - 126
- Pages
- 6
- Journal Title
- FEBS LETTERS
- Volume
- 577
- Number
- 1-2
- Start Page
- 121
- End Page
- 126
- URI
- https://scholarworks.bwise.kr/cau/handle/2019.sw.cau/24738
- DOI
- 10.1016/j.febslet.2004.10.004
- ISSN
- 0014-5793
1873-3468
- Abstract
- Hepatitis B virus X protein (HBx) of the hepatitis B virus is strongly implicated in angiogenesis and metastasis during hepatocarcinogenesis. Previously, we reported that HBx enhances activity of hypoxia-inducible factor-1alpha (HIF-1alpha), a potent transactivator that induces angiogenic factors. Here, we delineate the structural region of HBx that potentiates HIF-1alpha. The carboxy-terminus of HBx increased the stability of HIF-1a protein, probably through inhibiting interaction with von Hippel-Lindau protein. Further, the carboxy-terminus of HBx enhanced the transactivation function of HIF-1alpha by enhancing its association with CREB binding protein (CBP). Finally, we demonstrated the physical association of HBx with the basic helix-loop-helix/PER-ARNT-SIM domain, the inhibitory domain, and the carboxy-terminal transactivation domain of HIF-1alpha in vivo. (C) 2004 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.
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