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Envelope surface glycoprotein gp120
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env
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HIV-1 gp120 activates forward trafficking and surface clustering of NMDA receptors in membrane micro domains by a PKA-dependent phosphorylation of the NR1 C-terminal Ser897, followed by a PKC-dependent phosphorylation of Ser896 |
PubMed
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env
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Down modulation of the interaction between HIV-1 gp120 and CD4 by TPA is blocked by protein kinase C (PKC) inhibitors, suggesting PKC may play an important role in HIV-1 infection |
PubMed
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env
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c-FLIPL inhibits Bax activation via modulating PKC expression at the transcriptional level involving AP-2 during gp120 treatment |
PubMed
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env
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Pre-treatment of endothelial cells with fibroblast growth factor 2 (FGF2) protects cells from HIV-1 gp120 angiotoxicity; this protection is regulated by crosstalk among the ERK, PI3K-AKT and PKC signaling pathways |
PubMed
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env
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Induction of apoptosis in cell cultures through binding of HIV-1 gp120 or gp160 to CXCR4 involves protein kinase C, basic fibroblast growth factor, caspase-3, and the pro-apoptotic molecule Bax |
PubMed
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env
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HIV-1 gp120 increases the levels of calcium-dependent and -independent PKC isozymes; the most striking change is observed in PKC-zeta isozyme levels |
PubMed
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env
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A specific interaction between CD4 and HIV-1 gp120 is required for phosphorylation of CD4, which could involve protein kinase C |
PubMed
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env
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IL-16 induces rapid translocation of PKC from the cytosol to the membrane in CD4+ cells; PKC inhibitors completely block IL-16-induced lymphocyte migration as well as the motile response induced by HIV-1 gp120 and anti-CD4 antibody binding to CD4 |
PubMed
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Envelope surface glycoprotein gp160, precursor
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env
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HIV-1 gp160-induced AP-1 complex formation is dependent upon protein tyrosine phosphorylation and is abolished by inhibitors of protein kinase C, but it is unaffected by calcium channel blockers or cyclosporine A |
PubMed
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Envelope transmembrane glycoprotein gp41
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env
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A synthetic peptide corresponding to cytoplasmic domain residues 828-848 of HIV-1 gp41 inhibits pKC-catalysed phosphorylation of a protein substrate |
PubMed
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env
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A synthetic peptide containing residues 581-597 from HIV-1 gp41 inhibits protein kinase C (pkC)-mediated phosphorylation of the CD3 gamma-chain in intact cells and directly inhibits partially purified pkC |
PubMed
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Nef
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nef
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PKCtheta is a downstream effector of LCK and is recruited by HIV-1 Nef to form the Nef/LCK/PKCtheta complex, which promotes HIV transcription |
PubMed
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nef
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The formation of Nef/LCK/PKCtheta complex activates the ERK MAPK signaling pathway |
PubMed
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nef
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Interactions between HIV-1 Nef and PKC isozymes in Jurkat cells show that Nef interacts preferentially with PKCtheta; the interaction of Nef and PKCtheta is independent of calcium, but enhanced by phospholipid activators of PKC |
PubMed
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Tat
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tat
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HIV-1 Tat relocalizes PRKCQ (PKC-theta) and RELA (NFkB) to the nucleus of Jurkat T cells that stably express Tat |
PubMed
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tat
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HIV-1 Tat induces phosphorylation of Threonine538 in PRKCQ (PKC-theta) in Jurkat T cells stably expressing Tat |
PubMed
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tat
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HIV-1 Tat activates PRKCQ (PKC-theta) kinase activity, which leads to RELA (NFkB), NRAS, RAF1, MAP2K1 (MEK1), MAP2K2 (MEK2), MAPK3 (ERK1), and MAPK1 (ERK2) activation, in Jurkat T cells that stably express Tat |
PubMed
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tat
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HIV-1 Tat upregulates PRKCQ (PKC-theta) expression in Jurkat T cells stably expressing Tat |
PubMed
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tat
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HIV-1 Tat activates protein kinase C, resulting in the induction of TNF-alpha, IL-6 and IL-10 expression and the secretion of MCP-1 |
PubMed
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tat
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Tat-triggered PKCdelta and PKCtheta activation results in the downstream signaling through the apoptosis pathways mediated by both ERK1/2 and caspase-3 |
PubMed
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tat
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Phospholipase C/protein kinase C signaling pathway-dependent phosphorylation of p44/42 and JNK MAP kinases participates partially in IL-1beta induction by TAT |
PubMed
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tat
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Protein kinase C is required for HIV-1 Tat-mediated transactivation of the viral LTR promoter, indicating protein kinase C regulates the process of HIV-1 transactivation and may play a role in the transition of HIV from latency to productive growth |
PubMed
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tat
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Protein kinase C phosphorylates HIV-1 Tat on serine residue 46 |
PubMed
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matrix
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gag
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Protein kinase C (PKC) phosphorylates HIV-1 Matrix on serine residue 111 resulting in a shift in localization of Matrix from the cytosol to the cellular membrane, suggesting a myristoyl-protein switch regulated by PKC phosphorylation |
PubMed
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retropepsin
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gag-pol
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Phosphorylation of human recombinant vimentin by PKC inhibits the proteolytic processing of the vimentin head domain by HIV-1 protease |
PubMed
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reverse transcriptase
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gag-pol
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HIV-1 RT heterodimer expressed in bacteria can be phosphorylated in vitro by several purified mammalian protein kinases including auto-activated protein kinase (PK), CKII, cytosolic protamine kinase (CPK), myelin basic protein kinase 1 (MBPK1), and PRKC |
PubMed
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