| http://purl.uniprot.org/citations/14985469 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/14985469 | http://www.w3.org/2000/01/rdf-schema#comment | "The catalytic domain of overexpressed protein kinase C (PKC)-delta mediates phorbol 12-myristate 13-acetate (PMA)-induced differentiation or apoptosis in appropriate model cell lines. To define the portions of the catalytic domain that are critical for these isozyme-specific functions, we constructed reciprocal chimeras, PKC-delta/epsilonV5 and -epsilon/deltaV5, by swapping the V5 domains of PKC-delta and -epsilon. PKC-delta/epsilonV5 failed to mediate PMA-induced differentiation of 32D cells, showing the essential nature of the V5 domain for PKC-delta's functionality. The other chimera, PKC-epsilon/deltaV5, endowed inactive PKC-epsilon with nearly all PKC-delta's apoptotic ability, confirming the importance of PKC-delta in this function. Green fluorescent protein (GFP)-tagged PKC-deltaV5 and -epsilon/deltaV5 in A7r5 cells showed substantial basal nuclear localization, while GFP-tagged PKC-epsilon and -delta/epsilonV5 showed significantly less, indicating that the V5 region of PKC-delta contains determinants critical to its nuclear distribution. PKC-epsilon/deltaV5-GFP showed much slower kinetics of translocation to membranes in response to PMA than parental PKC-epsilon, implicating the PKC-epsilonV5 domain in membrane targeting. Thus, the V5 domain is critical in several of the isozyme-specific functions of PKC-delta and -epsilon."xsd:string |
| http://purl.uniprot.org/citations/14985469 | http://purl.uniprot.org/core/author | "Lu G."xsd:string |
| http://purl.uniprot.org/citations/14985469 | http://purl.uniprot.org/core/author | "Larsson C."xsd:string |
| http://purl.uniprot.org/citations/14985469 | http://purl.uniprot.org/core/author | "Mischak H."xsd:string |
| http://purl.uniprot.org/citations/14985469 | http://purl.uniprot.org/core/author | "Wang Q.J."xsd:string |
| http://purl.uniprot.org/citations/14985469 | http://purl.uniprot.org/core/author | "Mushinski J.F."xsd:string |
| http://purl.uniprot.org/citations/14985469 | http://purl.uniprot.org/core/author | "Blumberg P.M."xsd:string |
| http://purl.uniprot.org/citations/14985469 | http://purl.uniprot.org/core/author | "Goerke A."xsd:string |
| http://purl.uniprot.org/citations/14985469 | http://purl.uniprot.org/core/author | "Schlapkohl W.A."xsd:string |
| http://purl.uniprot.org/citations/14985469 | http://purl.uniprot.org/core/date | "2004"xsd:gYear |
| http://purl.uniprot.org/citations/14985469 | http://purl.uniprot.org/core/name | "Mol Cancer Res"xsd:string |
| http://purl.uniprot.org/citations/14985469 | http://purl.uniprot.org/core/pages | "129-140"xsd:string |
| http://purl.uniprot.org/citations/14985469 | http://purl.uniprot.org/core/title | "The V5 domain of protein kinase C plays a critical role in determining the isoform-specific localization, translocation, and biological function of protein kinase C-delta and -epsilon."xsd:string |
| http://purl.uniprot.org/citations/14985469 | http://purl.uniprot.org/core/volume | "2"xsd:string |
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