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The X protein of hepatitis B virus binds to the F box protein Skp2 and inhibits the ubiquitination and proteasomal degradation of c‐Myc
Author(s) -
Kalra Neetu,
Kumar Vijay
Publication year - 2006
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2005.12.034
Subject(s) - ubiquitin , f box protein , protein degradation , degradation (telecommunications) , skp2 , chemistry , virology , microbiology and biotechnology , biology , biochemistry , ubiquitin ligase , gene , telecommunications , computer science
The HBx protein of hepatitis B virus is involved in deregulation of cell cycle and development of hepatocellular carcinoma. Since c‐Myc also plays an important role in cell proliferation and tumor development, we studied its regulation by HBx in a human hepatoma cell line. Co‐expression of HBx and c‐Myc resulted in increased stability of intracellular c‐Myc. HBx blocked the ubiquitination of Myc through a direct interaction with the F box region of Skp2 and destabilization of the SCF Skp2 complex. We suggest that sustained presence of c‐Myc combined with mitogenic activity inherent to HBx may be associated with cell cycle deregulation and transformation.