Source:http://linkedlifedata.com/resource/entrezgene/hivinteraction/155807-9730
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rdf:type | |
entrezgene:pubmed |
pubmed-article:11223251,
pubmed-article:17314515,
pubmed-article:17559673,
pubmed-article:17609381,
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pubmed-article:8195203
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entrezgene:interactant | |
entrezgene:geneRifText |
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,
DCAF1 interacts with DDB1 as well as the Vpr-UNG2 complex, which leads to polyubiquitination of UNG2 via Vpr,
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,
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,
HIV-1 Vpr forms nuclear foci containing VPRBP and partially co-localizes with DNA repair foci components 53BP1 and phosphorylated RPA32,
HIV-1 Vpr significantly downregulates expression level of MFN2 in the mitochondria via VprBP-DDB1-CUL4A ubiquitin ligase in a proteasome-dependent manner,
HIV-1 Vpr(Q65R) mutant fails to bind DDB1 and VprBP, and also fails to induce G2 arrest,
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,
The interaction between Vpr and the Cul4A-DDB1-VprBP complex is required for the induction of G2 arrest,
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,
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,
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
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entrezgene:keyphrase |
interacts with,
cooperates with,
co-localizes with,
binds
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