Ubiquitination of APOBEC3G by an HIV-1 Vif-Cullin5-Elongin B-Elongin C complex is essential for Vif function.

@article{Kobayashi2005UbiquitinationOA,
  title={Ubiquitination of APOBEC3G by an HIV-1 Vif-Cullin5-Elongin B-Elongin C complex is essential for Vif function.},
  author={Masayuki Kobayashi and Akifumi Takaori-Kondo and Yasuhiro Miyauchi and Kazuhiro Iwai and Takashi Uchiyama},
  journal={The Journal of biological chemistry},
  year={2005},
  volume={280 19},
  pages={18573-8}
}
The human immunodeficiency virus type 1 (HIV-1) virion infectivity factor (Vif) overcomes the antiviral activity of APOBEC3G to protect HIV-1 DNA from G-to-A hypermutation. Vif targets APOBEC3G for ubiquitination and proteasomal degradation by forming an SCF-like E3 ubiquitin ligase complex composed of Cullin5, Elongin B, and Elongin C (Vif-BC-Cul5) through a novel SOCS-box motif. In this paper, we have established an in vitro ubiquitin conjugation assay with purified Vif-BC-Cul5 complex and… CONTINUE READING
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