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Envelope surface glycoprotein gp120
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env
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HIV-1 gp120 activates LIMK1/2 by increased levels of LIMK1/2 phosphorylation. Gp120-mediated LIMK activation is dependent on the Rack-PAK-LIMK pathway through phosphorylation of PAK2 and Rac1 |
PubMed
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Nef
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nef
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HIV-1 Nef requires the GTPase interaction site of PAK2 to facilitate interactions of Nef with EXOC |
PubMed
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nef
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HIV-1 Nef requires PAK2 for the Nef-EXOC interaction |
PubMed
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nef
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HIV-1 Nef-mediated PAK2 activation is found in multiple human cell lines of myeloid, lymphoid, and non-hematopoietic origin |
PubMed
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nef
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The activation of PAK2 by HIV-1 Nef is critical for human intrathymic T-cell development |
PubMed
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nef
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The association of HIV-1 Nef with PAK2 is important for enhancing activation of primary CD4/CD8+ T cells |
PubMed
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nef
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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 |
PubMed
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nef
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The Nef/hnRNPK/PKC-delta/Hck protein complex activates Pak2 activity but inhibits Pak1 activity, which induces paxillin phosphorylation on Ser272/274 and regulates paxillin/TACE association and secretion |
PubMed
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nef
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HIV-1 Nef induces increased levels of Pak2 phosphorylation at positions serine 192/197 |
PubMed
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nef
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HIV-1 Nef induces phosphorylation of MEK1 at position serine 298, which depends on Pak and Rac activity. The SH3 region mutation 72PXXP/AXXA75 in Nef results in loss of Pak association which decreases Nef-induced MEK1 phosphorylation |
PubMed
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nef
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The association of HIV-1 Nef with Vav1, Pak2, and Nck1 is greatly reduced in SLP76-deficient T cells |
PubMed
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nef
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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 |
PubMed
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nef
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The HIV-1 Nef highly conserved valine-glycine-phenylalanine amino acid triplet (VGF) motif is important for Nef-PAK2 association and cofilin hyper-phosphorylation |
PubMed
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nef
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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 |
PubMed
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nef
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HIV-1 Nef inactivates cofilin by inducing its hyperphosphorylation via association with PAK2 activity |
PubMed
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nef
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HIV-1 Nef requires a PAK2 recruitment motif (F195/191I) for inhibition of actin remodeling and induction of cofilin hyperphosphorylation |
PubMed
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nef
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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 |
PubMed
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nef
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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 |
PubMed
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nef
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HIV-1 group N and group O nef alleles interact with PAK-2, albeit with different efficiencies |
PubMed
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nef
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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) |
PubMed
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nef
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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 |
PubMed
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nef
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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 |
PubMed
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matrix
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gag
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hPAK65 has been demonstrated to phosphorylate HIV-1 Matrix on serine residues in vitro |
PubMed
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