The carboxy-terminus of the hepatitis B virus X protein is necessary and sufficient for the activation of hypoxia-inducible factor-1alpha.
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-1alpha 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.
Mesh Terms:
Animals, Blotting, Western, Cell Line, Humans, Hypoxia-Inducible Factor 1, alpha Subunit, Mice, Protein Binding, Trans-Activators, Transcription Factors, Transcription, Genetic
Animals, Blotting, Western, Cell Line, Humans, Hypoxia-Inducible Factor 1, alpha Subunit, Mice, Protein Binding, Trans-Activators, Transcription Factors, Transcription, Genetic
FEBS Lett.
Date: Nov. 05, 2004
PubMed ID: 15527772
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