Diaz-Meco MT et al. (1993), A dominant negative protein kinase C zeta subsp...

XB-ART-22358

Mol Cell Biol 1993 Aug 01;138:4770-5. doi: 10.1128/mcb.13.8.4770-4775.1993.

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A dominant negative protein kinase C zeta subspecies blocks NF-kappa B activation.

Diaz-Meco MT , Berra E , Municio MM , Sanz L , Lozano J , Dominguez I , Diaz-Golpe V , Lain de Lera MT , Alcamí J , Payá CV , Arenzana-Seisedos F , Virelizier JL , Moscat J .

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Nuclear factor kappa B (NF-kappa B) plays a critical role in the regulation of a number of genes. NF-kappa B is a heterodimer of 50- and 65-kDa subunits sequestered in the cytoplasm complexed to inhibitory protein I kappa B. Following stimulation of cells, I kappa B dissociates from NF-kappa B, allowing its translocation to the nucleus, where it carries out the transactivation function. The precise mechanism controlling NF-kappa B activation and the involvement of members of the protein kinase C (PKC) family of isotypes have previously been investigated. It was found that phorbol myristate acetate, (PMA) which is a potent stimulant of phorbol ester-sensitive PKC isotypes, activates NF-kappa B. However, the role of PMA-sensitive PKCs in vivo is not as apparent. It has recently been demonstrated in the model system of Xenopus laevis oocytes that the PMA-insensitive PKC isotype, zeta PKC, is a required step in the activation of NF-kappa B in response to ras p21. We demonstrate here that overexpression of zeta PKC is by itself sufficient to stimulate a permanent translocation of functionally active NF-kappa B into the nucleus of NIH 3T3 fibroblasts and that transfection of a kinase-defective dominant negative mutant of zeta PKC dramatically inhibits the kappa B-dependent transactivation of a chloramphenicol acetyltransferase reporter plasmid in NIH 3T3 fibroblasts. All these results support the notion that zeta PKC plays a decisive role in NF-kappa B regulation in mammalian cells.

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Species referenced: Xenopus laevis
Genes referenced: cdkn1a nsg1

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