Statements in which the resource exists as a subject.
PredicateObject
rdf:type
entrezgene:pubmed
pubmed-article:10607567, pubmed-article:11070003, pubmed-article:11160719, pubmed-article:11448168, pubmed-article:11463741, pubmed-article:12734410, pubmed-article:12855553, pubmed-article:14965316, pubmed-article:15047825, pubmed-article:15194762, pubmed-article:15638726, pubmed-article:15847608, pubmed-article:16272310, pubmed-article:16282498, pubmed-article:16501114, pubmed-article:16687395, pubmed-article:16912329, pubmed-article:16916529, pubmed-article:16979207, pubmed-article:17077296, pubmed-article:17586321, pubmed-article:17632197, pubmed-article:17632570, pubmed-article:17707624, pubmed-article:17881449, pubmed-article:18030346, pubmed-article:18094167, pubmed-article:18653452, pubmed-article:18808677, pubmed-article:19324886, pubmed-article:19683683, pubmed-article:20147394, pubmed-article:20594957, pubmed-article:21336563, pubmed-article:21819585, pubmed-article:21892329, pubmed-article:22103831, pubmed-article:22103837, pubmed-article:22103838, pubmed-article:22175768, pubmed-article:22323535, pubmed-article:22534017, pubmed-article:22537596, pubmed-article:22651890, pubmed-article:22844345, pubmed-article:9075929
entrezgene:interactant
entrezgene:geneRifText
Co-fractionation, 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
entrezgene:interactionSourc...
BioGRID
entrezgene:keyphrase
interacts with, co-localizes with, binds, associates with, activates, regulates, complexes with