Selective Assembly of HIV-1 Vif-Cul5-ElonginB-ElonginC E3 Ubiquitin Ligase Complex Through a Novel SOCS Box and Upstream Cysteines

Overview

Journal Genes Dev

Specialty Molecular Biology

Date 2004 Dec 3

PMID 15574593

Citations 180

Authors

Yunkai Yu

Zuoxiang Xiao

Elana S Ehrlich

Xianghui Yu

Xiao-Fang Yu

Affiliations

Soon will be listed here.

Abstract

APOBEC3G, which induces hypermutations in newly synthesized viral DNA, is suppressed by HIV-1 Vif, acting through Cul5-ElonginB-ElonginC E3 ubiquitin ligase. We have now characterized a novel SOCS box in HIV-1 Vif that mediates its interaction with ElonginC. In this SOCS box, alanine replaces the consensus cysteine in the previously identified SOCS box. This new motif was necessary but insufficient for interaction with Cul5-ElonginB-ElonginC, as two highly conserved Cys residues outside the SOCS box were required to interact with Cul5 but not ElonginC. Therefore, selective assembly with Cul5 versus Cul2 E3 may require protein interfaces besides the SOCS-box-ElonginC interaction.

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