The X protein of hepatitis B virus binds to the F box protein Skp2 and inhibits the ubiquitination and proteasomal degradation of c‐Myc | Zendy

Kalra Neetu | Zendy; Kumar Vijay | Zendy

Premium

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) - hbx , ubiquitin , skp2 , cell cycle , cell growth , chemistry , cell culture , cancer research , protein degradation , microbiology and biotechnology , hepatitis b virus , biology , cell , virus , virology , ubiquitin ligase , biochemistry , gene , genetics

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.

This content is not available in your region!

Continue researching here.

Having issues? You can contact us here

Accelerating Research