Source:http://linkedlifedata.com/resource/entrezgene/hivinteraction/156110-5062
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rdf:type | |
entrezgene:pubmed |
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pubmed-article:11070003,
pubmed-article:11160719,
pubmed-article:11448168,
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pubmed-article:15194762,
pubmed-article:15638726,
pubmed-article:15847608,
pubmed-article:16272310,
pubmed-article:16282498,
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pubmed-article:16687395,
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pubmed-article:16979207,
pubmed-article:17077296,
pubmed-article:17586321,
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pubmed-article:18653452,
pubmed-article:18808677,
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pubmed-article:19683683,
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pubmed-article:22651890,
pubmed-article:22844345,
pubmed-article:9075929
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entrezgene:interactant | |
entrezgene:geneRifText |
Fusing GFP to the C-terminal end of Nef results in a reduction in the level of activated PAK-2 associated with Nef. The impaired PAK-2 activation with Nef-GFP is due to the large size of the GFP fusion protein,
HIV-1 Nef binds to p21-activated kinase 2 (PAK2); this interaction is mediated through the N-terminal domain of Nef and the C-terminal part of the regulatory domain of PAK2,
HIV-1 Nef co-localizes with PAK-2 in lipid rafts; a palmitoylated Nef is highly enriched in lipid rafts and associates with higher levels of PAK-2 activity than wild type Nef,
HIV-1 Nef inactivates cofilin by inducing its hyperphosphorylation via association with PAK2 activity,
HIV-1 Nef requires a PAK2 recruitment motif (F195/191I) for inhibition of actin remodeling and induction of cofilin hyperphosphorylation,
HIV-1 Nef-mediated PAK2 activation is found in multiple human cell lines of myeloid, lymphoid, and non-hematopoietic origin,
HIV-1 group N and group O nef alleles interact with PAK-2, albeit with different efficiencies,
Hck-derived SH3 domains efficiently associate with HIV-1 Nef in cells and thereby potently inhibit SH3-dependent Nef functions, such as binding p21-activated kinase-2 (PAK2),
Mutation of HIV-1 Nef amino acid residues at positions 85, 89, 187, 188, and 191 dramatically alters association with Pak2 without affecting Nef expression levels or CD4 and MHC-I downregulation,
Nef-mediated microdomain recruitment of Vav1 is associated with the Nef-p21-activated kinase 2 (PAK2) signalosome. Nef residue F195 is identified as critical for Nef-mediated raft recruitment of Vav1,
The HIV-1 Nef highly conserved valine-glycine-phenylalanine amino acid triplet (VGF) motif is important for Nef-PAK2 association and cofilin hyper-phosphorylation,
The activation of PAK2 by HIV-1 Nef is critical for human intrathymic T-cell development,
The association of HIV-1 Nef with PAK2 is important for enhancing activation of primary CD4/CD8+ T cells,
The association of HIV-1 Nef with Vav1, Pak2, and Nck1 is greatly reduced in SLP76-deficient T cells,
The binding of HIV-1 Nef to the SH3 domain of Hck is required for Nef/activated PAK2 complex formation. A new locus GFP/F (G67, F68, P69 and F90) of Nef is involved in the Nef/activated PAK2 complex formation,
The mutation of all four glutamates (amino acids 62-65) to alanine in HIV-1 Nef impairs the ability of Nef to regulate p21-activated protein kinase 2 (PAK-2) and enhance viral particle infectivity
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entrezgene:keyphrase |
interacts with,
co-localizes with,
binds,
associates with,
activates,
regulates,
complexes with
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