The regulatory domain of protein kinase Cθ localises to the Golgi complex and induces apoptosis in neuroblastoma and Jurkat cells
- 22 May 2003
- journal article
- Published by Springer Nature in Cell Death & Differentiation
- Vol. 10 (6) , 662-675
- https://doi.org/10.1038/sj.cdd.4401235
Abstract
This study investigates apoptotic effects of protein kinase C (PKC) and in neuroblastoma cells. 12-O-tetradecanoylphorbol-13-acetate induces apoptosis in SK-N-BE(2) neuroblastoma cells overexpressing PKC or PKC, but not PKC. The PKC inhibitor GF109203X does not suppress this apoptotic effect, suggesting that it is independent of the catalytic activity of PKC. The isolated catalytic domains of PKC and PKC or the regulatory domain (RD) of PKC also induce apoptosis in neuroblastoma cells. The apoptotic responses are suppressed by caspase inhibition and by Bcl-2 overexpression. The PKC RD induced apoptosis also in Jurkat cells. Colocalisation analysis revealed that the PKC RD primarily localises to the Golgi complex. The C1b domain is required for this localisation and removal of the C1b domain results in a PKC construct that does not induce apoptosis. This suggests that the PKC RD has apoptotic activity and that Golgi localisation may be important for this effect.Keywords
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