The assembly of Vif ubiquitin E3 ligase for APOBEC3 degradation

Title
The assembly of Vif ubiquitin E3 ligase for APOBEC3 degradation
Author(s)
김동영
Keywords
HUMAN-IMMUNODEFICIENCY-VIRUS; HIV-1 REVERSE TRANSCRIPTION; VIRION INFECTIVITY FACTOR; AMINO-ACID DIFFERENCE; SOCS-BOX; TYPE-1 VIF; CBF-BETA; CRYSTAL-STRUCTURE; BINDING DOMAIN; ZINC-BINDING
Issue Date
201504
Publisher
PHARMACEUTICAL SOC KOREA
Citation
ARCHIVES OF PHARMACAL RESEARCH, v.38, no.4, pp.435 - 445
Abstract
APOBEC3G is a cellular antiviral protein that restricts retroviral infection. In non-permissive cells infected by Vif-deficient HIV-1, the protein mediates the hypermutation of viral DNA through the enzymatic activity of cytidine deaminase. To counteract the antiviral activity of APOBEC3G, an accessory protein of HIV-1, Vif, forms ubiquitin E3 ligase through assembly with CUL5-RBX2, ELOB-ELOC and CBF beta. Subsequently, Vif recruits APOBEC3G to the complex as a substrate adaptor of ubiquitin E3 ligase and induces poly-ubiquitination of APOBEC3G for its proteasomal degradation (Fig. 1). This review briefly summarizes current understanding of protein-protein interaction between Vif and host factors required for APOBEC3 degradation, based on high resolution structures of APOBEC3 proteins and Vif-CUL5NTD-ELOBC-CBF beta complex.
URI
http://hdl.handle.net/YU.REPOSITORY/32683http://dx.doi.org/10.1007/s12272-014-0519-x
ISSN
0253-6269
Appears in Collections:
약학대학 > 약학부 > Articles
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