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Envelope surface glycoprotein gp120
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env
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Env-dependent MDM/T cell viral synapse formation is facilitated by Vpr/VPRBP (DCAF1) cooperation |
PubMed
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env
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VPRBP (DCAF1) is required for HIV-1 Vpr to increase virion production (Gag/pr55 levels) and Env/gp160 (gp120/gp41) expression in MDM cells |
PubMed
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Envelope surface glycoprotein gp160, precursor
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env
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DCAF1 is required for HIV-1 Vpr to increase virion production (Gag/pr55 levels) and Env/gp160 (gp120/gp41) expression in MDM cells |
PubMed
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Envelope transmembrane glycoprotein gp41
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env
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Env-dependent MDM/T cell viral synapse formation is facilitated by Vpr/VPRBP (DCAF1) cooperation |
PubMed
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env
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VPRBP (DCAF1) is required for HIV-1 Vpr to increase virion production (Gag/pr55 levels) and Env/gp160 (gp120/gp41) expression in MDM cells |
PubMed
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Pr55(Gag)
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gag
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DCAF1 is required for HIV-1 Vpr to increase virion production (Gag/pr55 levels) and Env/gp160 (gp120/gp41) expression in MDM cells |
PubMed
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Vpr
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vpr
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Vpr-dependent HIV-1 spread from MDMs to CD4+ T lymphocytes requires VPRBP (DCAF1) |
PubMed
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vpr
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Vpr cooperates with VPRBP (DCAF1) to increase T lymphocyte HIV-1 infection by counteracting type I interferon inducible restriction of Env-dependent viral synapse formation between MDM and T cells |
PubMed
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vpr
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HIV-1 Vpr binds DCAF1; Vpr E25,L26 and a2 E29 form a small pocket for DCAF1 W1156 binding (the N-terminal tail of Vpr wraps around the propeller, following small groove between two blades) |
PubMed
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vpr
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HIV-1 Vpr binds DCAF1; residues R62, Q65 and R73 on a3 of Vpr form hydrogen bonds with E1088, S1136 and T1139 of DCAF1, respectively. Vpr F69 inserts in a small hydrophobic pocket formed by DCAF1 A1137, F1330 and F1355 |
PubMed
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vpr
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DCAF1 is required for HIV-1 Vpr to increase virion production (Gag/pr55 levels) and Env gp160 (gp120/gp41) expression in MDM cells |
PubMed
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vpr
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Residues N1135 and W1156 in DCAF1 are required for its binding to the SIVmac Vpx Q76 residue but not with HIV-1 Vpr |
PubMed
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vpr
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The minimal domain (residues 1041-1393) of DCAF1, which contains the motifs required for proper recruitment of both Vpr and DDB1, is not sufficient to support Vpr-mediated G2 arrest activity |
PubMed
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vpr
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The two WD-40 motifs (residues 1041-1393) in the C-terminal region of DCAF1 form a complex with HIV-1 Vpr and DDB1. The double mutant DCAF1 R1247/1283A completely abolishes its ability to bind both Vpr and DDB1 |
PubMed
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vpr
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The interaction of HIV-1 Vpr with the EDVP E3 ligase complex (EDD, DDB1, and VPRBP) promotes Vpr-mediated downregulation of TERT protein |
PubMed
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vpr
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HIV-1 Vpr directly interacts with the C-terminal SLX1 binding domain of SLX4 and recruits VPRBP to the SSE regulator complex SLX4 |
PubMed
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vpr
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Co-immunoprecipitation and glycerol-gradient sedimentation demonstrate that HIV-1 Vpr, VPRBP, DDB1, SLX4, MUS81, EME1, ERCC1, and ERCC4 form a complex |
PubMed
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vpr
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HIV-1 Vpr-mediated UNG2 degradation and constitutive UNG2 turnover are dependent on DCAF1 or DDB1 but not on CUL4a or CUL4B in the cullin4 (CUL4)-containing ubiquitin ligase complex in HEK293T cells |
PubMed
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vpr
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HIV-1 Vpr complexes with DCAF1, DDB1, CUL4A, CUL4B, and UNG2 proteins in the cullin4 (CUL4)-containing ubiquitin ligase complex in HEK293T cells |
PubMed
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vpr
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Mutation of Trp18, Gln65, and His71 residues in HIV-1 Vpr abrogates DDB1-DCAF1 binding and Vpr-induced cell cycle arrest |
PubMed
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vpr
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VPRBP is required for HIV-1 Vpr-mediated activation of the SLX4 complex and modulation of MUS81 levels. The interaction between Vpr and VPRBP is involved in MUS81 ubiquitination |
PubMed
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vpr
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HIV-1 Vpr-induced downregulation of Dicer is not dependent on G2 cell cycle arrest but on the Cul4A-DCAF1-DDB1 ubiquitin ligase complex |
PubMed
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vpr
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HIV-1 Vpr induces the degradation of ZIP/sZIP through the DCAF1 ubiquitin ligase, while VprQ65R mutant impairs the Vpr-induced degradation of ZIP/sZIP |
PubMed
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vpr
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HIV-1 Vpr co-localizes with the Cul4A ubiquitin ligase complex (Cul4A, DCAF1, and DDB1) in the cellular chromatin compartment |
PubMed
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vpr
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HIV-1 Vpr induces the degradation of APOBEC3G through VprBP binding and participation of the proteasome, leading to a reduction in APOBEC3G encapsidation into virions |
PubMed
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vpr
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The interaction of HIV-1 Vpr with VprBP enhances HIV-1 infection in monocyte-derived dendritic cells |
PubMed
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vpr
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HIV-1 Vpr significantly downregulates expression level of MFN2 in the mitochondria via VprBP-DDB1-CUL4A ubiquitin ligase in a proteasome-dependent manner |
PubMed
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vpr
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Upregulation of NKG2D ligands is dependent on HIV-1 Vpr-mediated activation of the TAR DNA damage/stress pathway, which requires the recruitment of the Cul4/DDB1/DCAF1 E3 ubiquitin ligase complex |
PubMed
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vpr
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W54R/S79A Vpr mutant impairs to interact with UNG2, but is still able to recruit DCAF1. Three G2 arrest-defective Vpr mutants, Q65R, K27M, and S79A, can interact with DCAF1 |
PubMed
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vpr
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A highly conserved 18WxxxxFxxFxxxAFxH33 motif of the HIV-1 Vpr binds to DCAF1, leading to Vpr-induced G2 arrest. Vpr mutants L22S/L23S and V30S/V31S impair the ability to induce G2 arrest |
PubMed
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vpr
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HIV-1 Vpr binds DCAF1 and activates the DNA damage response in renal tubule epithelial cells, in which gamma H2AX-positive nuclei are abundant compared to the control |
PubMed
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vpr
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DCAF1 interacts with DDB1 as well as the Vpr-UNG2 complex, which leads to polyubiquitination of UNG2 via Vpr |
PubMed
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vpr
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Recruitment of a catalytically active CRL4A (VPRBP) complex is required to observe HIV-1 Vpr-interacting unknown cellular ubiquitinated proteins. Phosphorylation of H2AX requires Vpr-induced K48 residue polyubiquitination |
PubMed
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vpr
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HIV-1 Vpr forms nuclear foci containing VPRBP and partially co-localizes with DNA repair foci components 53BP1 and phosphorylated RPA32 |
PubMed
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vpr
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HIV-1 Vpr(Q65R) mutant fails to bind DDB1 and VprBP, and also fails to induce G2 arrest |
PubMed
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vpr
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The interaction between Vpr and the Cul4A-DDB1-VprBP complex is required for the induction of G2 arrest |
PubMed
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vpr
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HIV-1 Vpr binds a ternary complex composed of DDB1, DDA1, and VprBP, and modulates the interaction between the DDB1-DDA1-VprBP complex and other factors |
PubMed
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vpr
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The leucine/isoleucine-rich domain of HIV-1 Vpr (amino acids 60-81) mediates binding of Vpr to the C-terminal half of VprBP (amino acids 636-1507), resulting in the cytoplasmic retention of Vpr |
PubMed
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