Protein interactions
Protein |
Gene |
Interaction |
Pubs |
Nef
|
nef
|
HIV-1 (SF2) Nef downregulates PVR; downregulation is dependent upon the SH3 binding domain in Nef in A3.01 T cells and HeLa TZM-bl cells |
PubMed
|
|
nef
|
HIV-1 downregulates PVR on cell surface in a Nef-dependent manner. HIV-1 Vpu contributes to the activity of Nef on surface PVR downregulation |
PubMed
|
|
nef
|
The Nef proteins from HIV-1 M NL4-3, SIVcpz EK505, and SIVgor CP2139 but not from SIVgsn 166, HIV-1 N CK1.62, and P RBF168, are capable of inducing cell surface downregulation of CD155 |
PubMed
|
|
nef
|
HIV-1 Vpu and Nef are both required to alter the subcellular localization of CD155 in perinuclear compartments and thus interfere with the efficient transport of CD155 to the cell surface |
PubMed
|
|
nef
|
NK-cell mediated lysis of HIV-1-infected cells via the interaction between DNAM1 and PVR is reduced by HIV-1 Nef |
PubMed
|
Vpr
|
vpr
|
HIV-1 Vpr upregulates PVR expression during HIV-1 infection in CD4+ T-cells |
PubMed
|
|
vpr
|
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
|
Vpu
|
vpu
|
The Vpu proteins from HIV-1 M NL4-3 and SIVgor CP2139 but not from SIVgsn 166, SIVcpz EK505, HIV-1 N CK1.62, and P RBF168, are capable of inducing cell surface downregulation of CD155 |
PubMed
|
|
vpu
|
HIV-1 Vpu and Nef are both required to alter the subcellular localization of CD155 in perinuclear compartments, and thus interfere with the efficient transport of CD155 to the cell surface |
PubMed
|
|
vpu
|
The transmembrane domain of HIV-1 Vpu, particularly A10, A14, and A18, is required for cell surface downregulation of CD155, while the CK-2 phosphorylation sites and the second alpha-helix in the cytoplasmic domain are dispensable |
PubMed
|
|
vpu
|
HIV-1 Vpu contributes to the activity of Nef on surface PVR downregulation |
PubMed
|
Go to the HIV-1, Human Interaction Database