Source:http://linkedlifedata.com/resource/entrezgene/interaction/920-155945
| Predicate | Object |
|---|---|
| rdf:type | |
| entrezgene:pubmed |
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| entrezgene:interactant | |
| entrezgene:geneRifText |
A simian-human immunodeficiency virus (SHIVtm) with a scrambled amino acid sequence in the transmembrane domain of HIV-1 Vpu fails to downregulate cell surface expression of CD4,
Affinity Capture-Western; FRET,
Cell surface CD4 inhibits HIV-1 particle release by interfering with Vpu activity, possibly by disrupting the oligomeric structure of Vpu,
Co-expression of HIV-1 Vpu with beta-TrCP2 induces degradation of total cellular CD4 content; Vpu-mediated CD4 down-modulation is inhibited by double silencing of beta-TrCP1 and beta-TrCP2,
Downregulation of CD4 and BST2 by HIV-1 Vpu is observed in HIV-1 infected humanized mice,
Downregulation of CD4 from the surface of HIV-1 infected cells by HIV-1 Vpu increases viral infectivity,
HIV-1 Vpu Y35A/L39G mutant has a significant increase in CD4 surface expression compared to wild-type Vpu,
HIV-1 Vpu from subtype P can downregulate CD4 from cell surface,
HIV-1 Vpu interacts with CD4 in living cells,
HIV-1 Vpu mediated degradation of CD4 requires the function of proteasomes and results from the formation of a ternary complex between beta-TrCP, Vpu and CD4 which connects CD4 to the endoplasmic reticulum degradation pathway,
HIV-1 Vpu mediates retention of CD4 in the ER. Transmembrane domain interactions are the main determinant of ER retention of CD4 by Vpu,
HIV-1 Vpu proteins from pandemic HIV-1 M strains, but not from nonpandemic HIV-1 N strains, degrade the viral receptor CD4,
HIV-1 Vpu regulates the formation of intracellular HIV-1 gp160-CD4 complexes and liberates Golgi-targeted gp160 from CD4-dependent retention in the endoplasmic reticulum,
Mutation of the HIV-1 Vpu Trp22 does not prevent Vpu-CD4 interaction but enhances Vpu oligomerization. The CD4 Gly415 residue within the CD4 TMD is required for both Vpu-CD4 interaction and Vpu-induced CD4 degradation,
NMR analysis indicates that amino acids (residues 39-48 and 64-70) in both helices of the HIV-1 Vpu cytoplasmic region are important for its binding to CD4,
Phosphorylation of HIV-1 Vpu on two serine phosphoacceptor sites (amino acids 52 and 56) by casein kinase 2 is required for Vpu-mediated degradation of CD4 in the endoplasmic reticulum,
Poly-ubiquitination of the CD4 cytosolic tail by SCFbeta-TrCP is required for HIV-1 Vpu-induced CD4 degradation,
Replication-defective Vpu TM mutants (V9D and I19D) and cytoplasmic domain mutants (S56G and E59K) fail to downregulate cell surface CD4, suggesting that viral replication potential and ability to downregulate CD4 by Vpu are correlated,
The C-terminal domain of HIV-1 Vpu (amino acids 76-81) interacts with the cytoplasmic domain of CD4 (amino acids 402-425) and causes the rapid degradation of CD4 in the endoplasmic reticulum,
The HIV-1 Vpu Trp22 mutation in the Vpu transmembrane domain fails to induce CD4 degradation by reduced CD4 polyubiquitination. The Trp residue is highly conserved in all HIV-1 Vpu variants, including those of HIV-1 groups M, N, and O,
The VCP-UFD1L-NPL4 complex is required for HIV-1 Vpu-induced CD4 degradation in the ER-associated degradation pathway. The ATPase activity of VCP and ubiquitin binding to UFD1L are important for CD4 degradation by Vpu,
The Val20 and Ser23 residues within the Vpu TMD are critical for Vpu-induced CD4 retention in the ER,
The invariant leucine 63 and the valine 68 within the predicted second alpha-helical domain of the HIV-1 Vpu cytoplasmic tail are required for CD4 down-modulation. L63A and V68A mutants still bind CD4 and retain the ability to interact with beta-TrCP1,
The putative cholesterol recognition amino acid consensus (CRAC) motif (residues 25-31) of HIV-1 Vpu mediates lipid raft association of Vpu and affects the downregulation of cell surface CD4
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| entrezgene:interactionSourc... |
BioGRID
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| entrezgene:keyphrase |
downregulates,
interacts with,
inhibited by
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