| pubmed-article:15781449 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:15781449 | lifeskim:mentions | umls-concept:C0019704 | lld:lifeskim |
| pubmed-article:15781449 | lifeskim:mentions | umls-concept:C0542341 | lld:lifeskim |
| pubmed-article:15781449 | lifeskim:mentions | umls-concept:C1519751 | lld:lifeskim |
| pubmed-article:15781449 | lifeskim:mentions | umls-concept:C1424930 | lld:lifeskim |
| pubmed-article:15781449 | lifeskim:mentions | umls-concept:C0205224 | lld:lifeskim |
| pubmed-article:15781449 | lifeskim:mentions | umls-concept:C0719053 | lld:lifeskim |
| pubmed-article:15781449 | pubmed:issue | 19 | lld:pubmed |
| pubmed-article:15781449 | pubmed:dateCreated | 2005-5-9 | lld:pubmed |
| pubmed-article:15781449 | pubmed:abstractText | 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 reported that the Vif-BC-Cul5 complex could function as an E3 ligase for APOBEC3G in vitro. A Vif-BC-Cul5 complex promotes the in vitro ubiquitination of the wild type, APOBEC3G but not that of D128K mutant, which does not interact with Vif. We have also investigated several loss-of-function Vif mutants. One mutant, SLQ144/146AAA, lost its activity on APOBEC3G because it could not form a complex due to mutations in SOCS-box motif. Other mutants, C114S and C133S, also lost their activity because of loss of the E3 ligase activity of a Vif-BC-Cul5 complex, although these mutants retained the ability to bind to APOBEC3G as well as Cul5 complex. These findings suggest that the E3 ubiquitin ligase activity of the Vif-BC-Cul5 complex is essential for Vif function against APOBEC3G. | lld:pubmed |
| pubmed-article:15781449 | pubmed:language | eng | lld:pubmed |
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| pubmed-article:15781449 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:15781449 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:15781449 | pubmed:month | May | lld:pubmed |
| pubmed-article:15781449 | pubmed:issn | 0021-9258 | lld:pubmed |
| pubmed-article:15781449 | pubmed:author | pubmed-author:UchiyamaTakas... | lld:pubmed |
| pubmed-article:15781449 | pubmed:author | pubmed-author:KobayashiMasa... | lld:pubmed |
| pubmed-article:15781449 | pubmed:author | pubmed-author:IwaiKazuhiroK | lld:pubmed |
| pubmed-article:15781449 | pubmed:author | pubmed-author:MiyauchiYasuh... | lld:pubmed |
| pubmed-article:15781449 | pubmed:author | pubmed-author:Takaori-Kondo... | lld:pubmed |
| pubmed-article:15781449 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:15781449 | pubmed:day | 13 | lld:pubmed |
| pubmed-article:15781449 | pubmed:volume | 280 | lld:pubmed |
| pubmed-article:15781449 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:15781449 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:15781449 | pubmed:pagination | 18573-8 | lld:pubmed |
| pubmed-article:15781449 | pubmed:dateRevised | 2007-11-15 | lld:pubmed |
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| pubmed-article:15781449 | pubmed:year | 2005 | lld:pubmed |
| pubmed-article:15781449 | pubmed:articleTitle | Ubiquitination of APOBEC3G by an HIV-1 Vif-Cullin5-Elongin B-Elongin C complex is essential for Vif function. | lld:pubmed |
| pubmed-article:15781449 | pubmed:affiliation | Department of Hematology and Oncology, Graduate School of Medicine, Kyoto University, 54 Shogoin-Kawaracho, Sakyo-ku, Kyoto 606-8507, Japan. | lld:pubmed |
| pubmed-article:15781449 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:15781449 | pubmed:publicationType | In Vitro | lld:pubmed |
| pubmed-article:15781449 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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