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Envelope surface glycoprotein gp120
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env
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HIV-1 gp120-treated vaginal epithelial cells show downregulation of protein kinase C, alpha (PRKCA) expression as compared to untreated control |
PubMed
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env
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HIV-1 gp120 activates forward trafficking and surface clustering of NMDA receptors in membrane microdomains 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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PKC-dependent pathway, particularly PKCalpha and PKCbeta1, requires HIV-1 gp120-mediated Rac-1 activation and membrane fusion |
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 Ca(2+) influx reduction is antagonized by an inhibitor acting especially on PKC alpha and PKC beta I; Western blotting analyses show that the cellular distribution of PKC alpha and -beta I are significantly modified by gp160 |
PubMed
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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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PKC activity and serine 6 in HIV-1 Nef are required for Nef-supported transcription, infectivity, and replication |
PubMed
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nef
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Treatment of cells with protein kinase C (PKC) inhibitors reduces HIV-1 Nef phosphorylation in vivo, and phosphorylation of Nef increases 8- to 12-fold after treatment with phorbol myristate acetate; these data indicate PKC phosphorylates Nef |
PubMed
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nef
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Protein kinase C phosphorylates HIV-1 Nef at threonine 15 |
PubMed
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Rev
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rev
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PKC has been shown to phosphorylate Rev in vitro, an effect associated with accelerated formation of an efficient RNA-binding conformation for Rev |
PubMed
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Tat
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tat
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The gene expression of protein kinase C alpha subunit is significantly upregulated in both clade B and clade C Tat treated SK-N-MC neuroblastoma cells |
PubMed
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tat
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HIV-1 Tat downregulates the expression of protein kinase C, alpha (PRKCA) in human primary T cells |
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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HIV-1 Tat-peptide(48-60) inhibits protein kinase C alpha and protein kinase A in a concentration-dependent manner |
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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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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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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matrix
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gag
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Protein kinase C (PKC) phosphorylates HIV-1 Gag and 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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