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Rev
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rev
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HIV-1 Rev interacting protein, Cullin 4A (CUL4A), is identified by the in-vitro binding experiments involving cytosolic or nuclear extracts from HeLa cells. The interaction of Rev with CUL4A is increased by RRE |
PubMed
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Vif
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vif
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Both HIV-1 Vif-induced downregulation of APOBEC3G and efficient infectivity in the presence of APOBEC3G requires CUL4A neddylation |
PubMed
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Vpr
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vpr
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Both HIV-2 Vpr and SIVmac239 Vpr induces G2 cell cycle arrest through either CUL4A or CUL4B |
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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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 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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Depletion of both CUL4A and CUL4B by shRNA reduces HIV-1 Vpr-mediated G2 cell cycle arrest, which does not impact HIV-1 infectivity or cell viability |
PubMed
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vpr
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HIV-1 Vpr-mediated degradation of UNG2 is dependent on CUL4A neddylation |
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-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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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 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 forms a complex by recruiting RbAp46, HAT1, ZIP/sZIP, and Cul4A |
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(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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