| Interacting proteins: P29966 and P17252 |
Pubmed |
SVM Score :0.0 |
| Dose response studies revealed that the most effective TPA concentration for stimulation of DNA synthesis and growth of melanocytes ( 10 ng / ml TPA ) also supported a relatively high level of PKC enzyme activity , increased membrane association of the PKC alpha and PKC epsilon isoforms , and led to a high level of phosphorylation of a major PKC substrate , the myristoylated alanine rich C kinase substrate ( MARCKS ) protein . ^^^ |
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| Interacting proteins: P29966 and P17252 |
Pubmed |
SVM Score :0.0 |
| However , while RA induced a five to eightfold increase in total cellular PKC alpha protein levels , it only increased MARCKS phosphorylation by twofold . ^^^ |
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| Interacting proteins: P29966 and P17252 |
Pubmed |
SVM Score :0.0 |
| We studied the distribution of MARCKS , the alpha isozyme of PKC ( PKC alpha ) , and myosin 1 in lipopolysaccharide treated peritoneal macrophages ingesting zymosan particles . ^^^ MARCKS , PKC alpha , and myosin 1 colocalized with F actin and talin in the cortical cytoplasm adjacent to forming phagocytic cups . ^^^ By contrast , MARCKS and PKC alpha remained associated with the phagosome membrane until after acquisition of the lysosomal marker Lamp 1 . ^^^ Inhibitors of PKC reduced zymosan binding to the macrophage surface and blocked the focal accumulation of F actin , talin , phosphotyrosine containing proteins , MARCKS , and PKC alpha beneath attached particles . ^^^ We propose that PKC dependent phosphorylation is an early signal required for zymosan phagocytosis and that MARCKS and PKC alpha have a role in phagosome maturation . ^^^ |
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| Interacting proteins: P29966 and P17252 |
Pubmed |
SVM Score :0.0 |
| Phosphorylation of three physiological substrates of protein kinase C ( PKC ) , MARCKS , neuromodulin ( Nm ) , and neurogranin ( Ng ) , was analyzed to determine their relative efficacy as substrates of PKC alpha , beta , and gamma and sensitivities to inhibition by calmodulin ( CaM ) and S 100 . ^^^ In contrast , the rates of PKC alpha catalyzed phosphorylation of Nm and Ng in a mixture also containing MARCKS were significantly reduced as compared to that when Nm or Ng was individually phosphorylated by this isozyme . ^^^ |
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| Interacting proteins: P29966 and P17252 |
Pubmed |
SVM Score :0.0 |
| Insulin provoked rapid increases in 1 ) diacylglycerol ; 2 ) translocation of PKC epsilon , but not PKC alpha , PKC delta , or PKC zeta , from the cytosol to the membrane fraction ; 3 ) membrane PKC enzyme activity ; and 4 ) phosphorylation of immunoprecipitable 80 kilodalton ( kDa ) myristylated alanine rich C kinase substrate ( MARCKS ) protein and heat stable 80 kDa protein ( also probably MARCKS ) . ^^^ |
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| Interacting proteins: P29966 and P17252 |
Pubmed |
SVM Score :0.0 |
| To address this question , we partially purified human MARCKS from baculovirus infected cells and compared the kinetic parameters for phosphorylation by PKC isozymes , conventional PKC alpha ( cPKC alpha ) , novel PKC delta ( nPKC delta ) , nPKC epsilon , and atypical PKC zeta ( apKC zeta ) , all of which are distributed in a wide variety of cells . cPKC alpha , nPKC delta , and nPKC epsilon efficiently phosphorylated intact MARCKS protein in vitro . ^^^ |
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| Interacting proteins: P29966 and P17252 |
Pubmed |
SVM Score :0.0 |
| To investigate the regulation of phorbol ester stimulated synthesis of phosphatidylcholine ( PtdCho ) , myristoylated alanine rich protein kinase C substrate ( MARCKS ) and the alpha isoform of protein kinase C ( PKC alpha ) were overexpressed in a human neuroblastoma ( SK N MC ) cell line that does not increase PtdCho synthesis in response to 4beta 12 O tetradecanoylphorbol 13 acetate ( TPA ) . ^^^ TPA caused translocation of PKC alpha and increased phosphorylation of MARCKS , indicating that both overexpressed proteins responded to stimulation . ^^^ Thus , in SK N MC cells , MARCKS is required for TPA stimulated synthesis of PtdCho and PKC alpha alone is insufficient for supporting enhanced synthesis . . ^^^ |
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| Interacting proteins: P29966 and P17252 |
Pubmed |
SVM Score :0.0 |
| Correlation with metabolism of membrane phospholipids suggests that PKC alpha and MARCKS may be required to mediate phosphatidylcholine turnover stimulated by phorbol ester ( beta TPA ) . ^^^ By day 4 , mRNA for PKC alpha and MARCKS increased and , after an initial decrease , PKC alpha protein also increased . ^^^ Thus , induced differentiation of human neuroblastoma cells involved increased expression of PKC alpha and MARCKS and synthesis of phosphatidylcholine , consistent with involvement of PKC alpha and MARCKS in regulation of phosphatidylcholine turnover during neurite growth . . ^^^ |
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| Interacting proteins: P29966 and P17252 |
Pubmed |
SVM Score :0.0 |
| MARCKS and PKC alpha were expressed at the plasma membrane of the neuroepithelial cells comprising the future neural tube , as well as in the surface ectoderm and underlying mesenchyme . ^^^ |
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| Interacting proteins: P29966 and P17252 |
Pubmed |
SVM Score :0.0 |
| Selective down regulation of PKC subtypes by prolonged exposure to phorbol 12 , 13 dibutyrate ( 100 nM ) attenuated the TPA induced enhancement of NA release and the translocation of MARCKS over an interval similar to that of down regulation of PKC alpha ( but not epsilon or zeta ) . ^^^ Thus , we have demonstrated a strong correlation between the translocation of MARCKS and the enhancement of NA release from SH SY5Y cells due to the TPA induced activation of PKC alpha . . ^^^ |
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| Interacting proteins: P29966 and P17252 |
Pubmed |
SVM Score :0.0 |
| Conventional PKC alpha , novel PKC epsilon and PKC theta , but not atypical PKC lambda are MARCKS kinases in intact NIH 3T3 fibroblasts . ^^^ Consistently , phorbol 12 , 13 dibutyrate dependent MARCKS phosphorylation was significantly reduced in cell lines expressing dominant negative mutants of either PKC alpha K368R or ( dominant negative ) PKC epsilon K436R . ^^^ |
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| Interacting proteins: P29966 and P17252 |
Pubmed |
SVM Score :0.0 |
| In contrast , CD treatment had no effect on phorbol ester stimulated phosphorylation of MARCKS or on translocation of PKC alpha to the membrane fraction . ^^^ Staurosporine inhibited the phorbol ester induced translocation of MARCKS but not of PKC alpha in both CD pretreated and untreated cells . ^^^ |
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| Interacting proteins: P29966 and P17252 |
Pubmed |
SVM Score :0.0 |
| Pretreatment of cells with 2 microM 4 beta 12 O tetradecanoyl phorbol 13 acetate ( beta TPA ) for 18 h downregulated conventional ( PKC alpha ) and novel ( PKC delta ) isoforms of PKC by > 90 % in both membrane and soluble fractions , but did not inhibit the rate of ATP dependent phosphorylation or release of MARCKS , or decrease levels of membrane bound PKC zeta or PKC mu . ^^^ |
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| Interacting proteins: P29966 and P17252 |
Pubmed |
SVM Score :0.0 |
| Chronic lithium administration produces a reduction in the expression of PKC alpha and epsilon , as well as a major PKC substrate , MARCKS , which has been implicated in long term neuroplastic events in the developing and adult brain . ^^^ |
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| Interacting proteins: P29966 and P17252 |
Pubmed |
SVM Score :0.0 |
| MARCKS PSD was more potent than another widely used selective PKC substrate ( neurogranin ( ( 28 43 ) ) and was a good substrate for human recombinant PKC alpha , delta , and epsilon but not zeta . ^^^ |
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| Interacting proteins: P29966 and P17252 |
Pubmed |
SVM Score :0.0 |
| Immunoprecipitation with an anti PKC theta antibody , but not with the antibodies against the other PKC isoforms , such as conventional PKC alpha , novel PKC delta , and novel PKC epsilon , inhibited phosphorylation of MARCKS . ^^^ |
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| Interacting proteins: P29966 and P17252 |
Pubmed |
SVM Score :0.0 |
| In addition , we examined the effects of retinoic acid on protein kinase C alpha ( PKC alpha ) and myristoylated alanine rich C kinase substrate ( MARCKS ) . ^^^ These data indicate that retinoid treatment causes inactivation of PKC alpha , allowing MARCKS to relocalize to the membrane , where it can cross link actin filaments . ^^^ |
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| Interacting proteins: P29966 and P17252 |
Pubmed |
SVM Score :0.0 |
| PKC alpha activated by Abeta directly phosphorylated a recombinant MARCKS in vitro , Translocation of PKC alpha from the cytoplasm to the membrane and accumulation of phospho MARCKS in the cytoplasm were induced by Abeta . ^^^ These results suggest involvement of a phosphoinositide signaling system through PKC alpha in the phosphorylation of MARCKS in neurons , an event which may be associated with mechanisms underlying neurotrophic and neurotoxic effects of Abeta . . ^^^ |
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| Interacting proteins: P29966 and P17252 |
Pubmed |
SVM Score :0.0 |
| In the present study , we tested full length DGK zeta and found that PKC alpha phosphorylated DGK zeta on serines within the MARCKS PSD in vitro and in vivo . ^^^ These results suggest that by phosphorylating the MARCKS PSD , PKC alpha attenuates DGK zeta activity . ^^^ |
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| Interacting proteins: P29966 and P17252 |
Pubmed |
SVM Score :0.0 |
| DCA also caused dramatic translocation of PH PLCdelta GFP , and conventional , Ca2+ / diacylglycerol ( DAG ) dependent isoforms of PKC ( PKC betaI and PKC alpha ) , and MARCKS GFP , but only in Ca2+ containing solutions . ^^^ |
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| Interacting proteins: P29966 and P17252 |
Pubmed |
SVM Score :0.0 |
| In other cell types , various isoforms of calpain , PKC alpha and MARCKS were found associated with caveolae . ^^^ Futhermore we provide evidence , using a calcium ionophore and a specific inhibitor of calpains ( calpastatin peptide ) , that milli calpain reduces the PKC alpha and MARCKS content in these structures . ^^^ Purified milli calpain causes the appearance of the active catalytic fragment of PKC alpha ( PKM ) , without having an effect on MARCKS . ^^^ Addition of phorbol myristate acetate , an activator of PKC , induces tranlocation of PKC alpha towards caveolae and results in a significant reduction of MARCKS associated with caveolae . ^^^ We conclude that the presence of biologically active milli calpain within myoblast caveolae induces , in a PKC alpha dependent manner , MARCKS translocation towards the cytosol . ^^^ |
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| Interacting proteins: P29966 and P17252 |
Pubmed |
SVM Score :0.0 |
| NA |
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| Interacting proteins: P29966 and P17252 |
Pubmed |
SVM Score :0.0 |
| NA |
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| Interacting proteins: P29966 and P17252 |
Pubmed |
SVM Score :0.0 |
| NA |
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| Interacting proteins: P29966 and P17252 |
Pubmed |
SVM Score :0.0 |
| NA |
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| Interacting proteins: P29966 and P17252 |
Pubmed |
SVM Score :0.0 |
| NA |
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| Interacting proteins: P29966 and P17252 |
Pubmed |
SVM Score :0.0 |
| NA |
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| Interacting proteins: P29966 and P17252 |
Pubmed |
SVM Score :0.0 |
| NA |
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| Interacting proteins: P29966 and P17252 |
Pubmed |
SVM Score :0.0 |
| NA |
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| Interacting proteins: P29966 and P17252 |
Pubmed |
SVM Score :0.0 |
| NA |
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| Interacting proteins: P29966 and P17252 |
Pubmed |
SVM Score :0.0 |
| NA |
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| Interacting proteins: P29966 and P17252 |
Pubmed |
SVM Score :0.0 |
| NA |
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| Interacting proteins: P29966 and P17252 |
Pubmed |
SVM Score :0.0 |
| NA |
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| Interacting proteins: P29966 and P17252 |
Pubmed |
SVM Score :0.0 |
| NA |
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| Interacting proteins: P29966 and P17252 |
Pubmed |
SVM Score :0.0 |
| NA |
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| Interacting proteins: P29966 and P17252 |
Pubmed |
SVM Score :0.0 |
| NA |
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| Interacting proteins: P29966 and P17252 |
Pubmed |
SVM Score :0.0 |
| NA |
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| Interacting proteins: P29966 and P17252 |
Pubmed |
SVM Score :0.0 |
| NA |
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| Interacting proteins: P29966 and P17252 |
Pubmed |
SVM Score :0.0 |
| NA |
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| Interacting proteins: P29966 and P17252 |
Pubmed |
SVM Score :0.0 |
| NA |
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| Interacting proteins: P29966 and P17252 |
Pubmed |
SVM Score :0.0 |
| NA |
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| Interacting proteins: P29966 and P17252 |
Pubmed |
SVM Score :0.0 |
| NA |
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| Interacting proteins: P29966 and P17252 |
Pubmed |
SVM Score :0.0 |
| NA |
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| Interacting proteins: P29966 and P17252 |
Pubmed |
SVM Score :0.0 |
| NA |
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| Interacting proteins: P29966 and P17252 |
Pubmed |
SVM Score :0.0 |
| NA |
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| Interacting proteins: P29966 and P17252 |
Pubmed |
SVM Score :0.0 |
| NA |
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| Interacting proteins: P29966 and P17252 |
Pubmed |
SVM Score :0.0 |
| NA |
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| Interacting proteins: P29966 and P17252 |
Pubmed |
SVM Score :0.0 |
| NA |
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| Interacting proteins: P29966 and P17252 |
Pubmed |
SVM Score :0.0 |
| NA |
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| Interacting proteins: P29966 and P17252 |
Pubmed |
SVM Score :0.0 |
| NA |
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| Interacting proteins: P29966 and P17252 |
Pubmed |
SVM Score :0.0 |
| NA |
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| Interacting proteins: P29966 and P17252 |
Pubmed |
SVM Score :0.0 |
| NA |
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