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Article

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

The Journal of biological chemistry - 13 May 2005

Kobayashi Masayuki, Takaori-Kondo Akifumi, Miyauchi Yasuhiro, Iwai Kazuhiro, Uchiyama Takashi

Abstract excerpt

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...

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Methodology Data sources Editorial policy Privacy Delete account & data About Contact Helena Bioinformatics

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Identifiers

PMID: 15781449
DOI: 10.1074/jbc.C500082200

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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Ubiquitination of APOBEC3G by an HIV-1 Vif-Cullin5-Elongin B-Elongin C complex is essential for Vif function.PMID 15781449Read ↗

Induction of APOBEC3G ubiquitination and degradation by an HIV-1 Vif-Cul5-SCF complex.Semantic proximity Read ↗

Structural insight into the human immunodeficiency virus Vif SOCS box and its role in human E3 ubiquitin ligase assembly.Semantic proximity Read ↗

Advances in the Structural Understanding of Vif ProteinsSemantic proximity Read ↗

Identification of a Cullin5-ElonginB-ElonginC E3 complex in degradation of feline immunodeficiency virus Vif-mediated feline APOBEC3 proteins.Semantic proximity Read ↗

Interactions between HIV-1 Vif and human ElonginB-ElonginC are important for CBF-β binding to VifSemantic proximity Read ↗

Distinct Determinants in HIV-1 Vif and Human APOBEC3 Proteins Are Required for the Suppression of Diverse Host Anti-Viral ProteinsSemantic proximity Read ↗

Characterization of conserved motifs in HIV-1 Vif required for APOBEC3G and APOBEC3F interaction.Semantic proximity Read ↗

Vif overcomes the innate antiviral activity of APOBEC3G by promoting its degradation in the ubiquitin-proteasome pathway.Semantic proximity Read ↗

Identification of dominant negative human immunodeficiency virus type 1 Vif mutants that interfere with the functional inactivation of APOBEC3G by virus-encoded Vif.Semantic proximity Read ↗

Characterization of the interaction of full-length HIV-1 Vif protein with its key regulator CBFβ and CRL5 E3 ubiquitin ligase components.Semantic proximity Read ↗

Various strategies for developing APOBEC3G protectors to circumvent human immunodeficiency virus type 1.Semantic proximity Read ↗

APOBEC3G is degraded by the proteasomal pathway in a Vif-dependent manner without being polyubiquitylated.Semantic proximity Read ↗

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