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http://purl.uniprot.org/citations/17579121http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/17579121http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/17579121http://www.w3.org/2000/01/rdf-schema#comment"Protein kinase Cdelta (PKCdelta) regulates cell apoptosis and survival in diverse cellular systems. PKCdelta translocates to different subcellular sites in response to apoptotic stimuli; however, the role of its subcellular localization in its proapoptotic and antiapoptotic functions is just beginning to be understood. Here, we used a PKCdelta constitutively active mutant targeted to the cytosol, nucleus, mitochondria, and endoplasmic reticulum (ER) and examined whether the subcellular localization of PKCdelta affects its apoptotic and survival functions. PKCdelta-Cyto, PKCdelta-Mito, and PKCdelta-Nuc induced cell apoptosis, whereas no apoptosis was observed with the PKCdelta-ER. PKCdelta-Cyto and PKCdelta-Mito underwent cleavage, whereas no cleavage was observed in the PKCdelta-Nuc and PKCdelta-ER. Similarly, caspase-3 activity was increased in cells overexpressing PKCdelta-Cyto and PKCdelta-Mito. In contrast to the apoptotic effects of the PKCdelta-Cyto, PKCdelta-Mito, and PKCdelta-Nuc, the PKCdelta-ER protected the cells from tumor necrosis factor-related apoptosis-inducing ligand-induced and etoposide-induced apoptosis. Moreover, overexpression of a PKCdelta kinase-dead mutant targeted to the ER abrogated the protective effect of the endogenous PKCdelta and increased tumor necrosis factor-related apoptosis-inducing ligand-induced apoptosis. The localization of PKCdelta differentially affected the activation of downstream signaling pathways. PKCdelta-Cyto increased the phosphorylation of p38 and decreased the phosphorylation of AKT and the expression of X-linked inhibitor of apoptosis protein, whereas PKCdelta-Nuc increased c-Jun NH(2)-terminal kinase phosphorylation. Moreover, p38 phosphorylation and the decrease in X-linked inhibitor of apoptosis protein expression played a role in the apoptotic effect of PKCdelta-Cyto, whereas c-Jun NH(2)-terminal kinase activation mediated the apoptotic effect of PKCdelta-Nuc. Our results indicate that the subcellular localization of PKCdelta plays important roles in its proapoptotic and antiapoptotic functions and in the activation of downstream signaling pathways."xsd:string
http://purl.uniprot.org/citations/17579121http://purl.org/dc/terms/identifier"doi:10.1158/1541-7786.mcr-06-0255"xsd:string
http://purl.uniprot.org/citations/17579121http://purl.org/dc/terms/identifier"doi:10.1158/1541-7786.mcr-06-0255"xsd:string
http://purl.uniprot.org/citations/17579121http://purl.uniprot.org/core/author"Lee H.K."xsd:string
http://purl.uniprot.org/citations/17579121http://purl.uniprot.org/core/author"Lee H.K."xsd:string
http://purl.uniprot.org/citations/17579121http://purl.uniprot.org/core/author"Lu W."xsd:string
http://purl.uniprot.org/citations/17579121http://purl.uniprot.org/core/author"Lu W."xsd:string
http://purl.uniprot.org/citations/17579121http://purl.uniprot.org/core/author"Xiang C."xsd:string
http://purl.uniprot.org/citations/17579121http://purl.uniprot.org/core/author"Xiang C."xsd:string
http://purl.uniprot.org/citations/17579121http://purl.uniprot.org/core/author"Brodie C."xsd:string
http://purl.uniprot.org/citations/17579121http://purl.uniprot.org/core/author"Brodie C."xsd:string
http://purl.uniprot.org/citations/17579121http://purl.uniprot.org/core/author"Finniss S."xsd:string
http://purl.uniprot.org/citations/17579121http://purl.uniprot.org/core/author"Finniss S."xsd:string
http://purl.uniprot.org/citations/17579121http://purl.uniprot.org/core/author"Gomel R."xsd:string
http://purl.uniprot.org/citations/17579121http://purl.uniprot.org/core/author"Gomel R."xsd:string
http://purl.uniprot.org/citations/17579121http://purl.uniprot.org/core/author"Okhrimenko H."xsd:string
http://purl.uniprot.org/citations/17579121http://purl.uniprot.org/core/author"Okhrimenko H."xsd:string
http://purl.uniprot.org/citations/17579121http://purl.uniprot.org/core/date"2007"xsd:gYear
http://purl.uniprot.org/citations/17579121http://purl.uniprot.org/core/date"2007"xsd:gYear
http://purl.uniprot.org/citations/17579121http://purl.uniprot.org/core/name"Mol. Cancer Res."xsd:string
http://purl.uniprot.org/citations/17579121http://purl.uniprot.org/core/name"Mol. Cancer Res."xsd:string
http://purl.uniprot.org/citations/17579121http://purl.uniprot.org/core/pages"627-639"xsd:string
http://purl.uniprot.org/citations/17579121http://purl.uniprot.org/core/pages"627-639"xsd:string
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