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- Title
Induction of APOBEC3G ubiquitination and degradation by an HIV-1 Vif-Cul5-SCF complex.
- Authors
Yu, Xianghui; Yu, Yunkai; Liu, Bindong; Luo, Kun; Kong, Wei; Mao, Panyong; Yu, Xiao-Fang
- Abstract
Human immunodeficiency virus-1 (HIV-1) Vif is essential for viral evasion of host antiviral factor CEM15/APOBEC3G. We report that Vif interacts with cellular proteins Cul5, elongins B and C, and Rbx1 to form an Skp1-cullin-F-box (SCF)-like complex. The ability of Vif to suppress antiviral activity of APOBEC3G was specifically dependent on Cul5-SCF function, allowing Vif to interact with APOBEC3G and induce its ubiquitination and degradation. A Vif mutant that interacted with APOBEC3G but not with Cul5-SCF was functionally inactive. The Cul5-SCF was also required for Vif function in distantly related simian immunodeficiency virus mac. These results indicate that the conserved Cul5-SCF pathway used by Vif is a potential target for antiviral development.
- Publication
Science (New York, N.Y.), 2003, Vol 302, Issue 5647, p1056
- ISSN
1095-9203
- Publication type
Journal Article
- DOI
10.1126/science.1089591