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Basic Characteristics of Mutations
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Mutation Site
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R118G |
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Mutation Site Sentence
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When the biotinylation proximity assay (Roux et al., 2012) was coupled to Western blot analysis, CCDC137 was found to be biotinylated by Vpr-BirA(R118G) but not BirA(R118G) despite our inability to detect biotinylated CCDC137 in the initial mass spectroscopic screens (Figure 3C). |
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Mutation Level
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Amino acid level |
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Mutation Type
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Nonsynonymous substitution |
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Gene/Protein/Region
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Vpr |
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Standardized Encoding Gene
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Vpr
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Genotype/Subtype
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HIV-1 |
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Viral Reference
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NL4-3
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Functional Impact and Mechanisms
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Disease
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HIV Infections
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Immune
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- |
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Target Gene
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-
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Clinical and Epidemiological Correlations
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Clinical Information
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- |
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Treatment
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- |
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Location
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- |
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Literature Information
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PMID
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32538781
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Title
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HIV-1 Vpr induces cell cycle arrest and enhances viral gene expression by depleting CCDC137
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Author
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Zhang F,Bieniasz PD
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Journal
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eLife
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Journal Info
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2020 Jun 15;9:e55806
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Abstract
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The HIV-1 Vpr accessory protein induces ubiquitin/proteasome-dependent degradation of many cellular proteins by recruiting them to a cullin4A-DDB1-DCAF1 complex. In so doing, Vpr enhances HIV-1 gene expression and induces (G2/M) cell cycle arrest. However, the identities of Vpr target proteins through which these biological effects are exerted are unknown. We show that a chromosome periphery protein, CCDC137/cPERP-B, is targeted for depletion by HIV-1 Vpr, in a cullin4A-DDB1-DCAF1 dependent manner. CCDC137 depletion caused G2/M cellcycle arrest, while Vpr-resistant CCDC137 mutants conferred resistance to Vpr-induced G2/M arrest. CCDC137 depletion also recapitulated the ability of Vpr to enhance HIV-1 gene expression, particularly in macrophages. Our findings indicate that Vpr promotes cell-cycle arrest and HIV-1 gene expression through depletion of CCDC137.
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Sequence Data
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-
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