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Rev
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rev
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HIV-1 Rev interacting protein, DNA damage-binding protein 1 (DDB1), is identified by the in-vitro binding experiments involving cytosolic or nuclear extracts from HeLa cells. The interaction of Rev with DDB1 is increased by RRE |
PubMed
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Vif
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vif
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HIV-1 Vif interacts with DDB1; interaction predicted to be relevant to proteolysis |
PubMed
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Vpr
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vpr
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DDB1-specific shRNA silencing demonstrates that DDB1 enhances TNF-alpha secretion from wild type HIV-1(NL43) infected AND delta-vpr HIV-infected MT4C5 cells suggesting that DDB1 enhances TNF-alpha release from HIV-1-infected cells independently of Vpr |
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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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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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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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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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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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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The interaction of Vpr with DDB1 facilitates the formation of complexes containing Cul4A-Roc1 E3 ubiquitin ligase. The association of Vpr with DDB1-containing E3 ligase mediates the degradation of UNG2 and SMUG1 |
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-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-mediated upregulation of PVR (CD155) requires the interaction of Vpr with the DDB1-Cul4A E3 ligase and induction of ATR-mediated DNA damage repair and G2 arrest |
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 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 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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HIV-1 Vpr binds the Cul4A-DDB1-VprBP complex and increases the levels of neddylated Cul4A in that complex only |
PubMed
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vpr
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DDB1 overexpression enables G2 cell cycle arrest by both HIV-1 Vpr and its carboxy-terminally truncated form C81 |
PubMed
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vpr
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HIV-1 Vpr(Q65R) mutant, which is defective in Cul4A-DDB1 (DCAF1) binding, undergoes proteasome-mediated degradation at a higher rate than wild-type Vpr. DCAF1 overexpression stabilizes wild-type Vpr and leads to its cytoplasmic accumulation |
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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HIV-1 Vpr interferes with the interaction of DDB1 and DDB2 in cells |
PubMed
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vpr
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HIV-1 Vpr interacts with damage-specific DNA-binding protein 1 (DDB1) in cells. L64P mutation in DDB1 fails to interact efficiently with Vpr |
PubMed
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