Cyclin-dependent kinase activating kinase/Cdk7 co-localizes with PKC-ι in human glioma cells

Cyclin-dependent kinase activating kinase (CAK) is a trimeric complex composed of cdk7, cyclin H and MAT1. CAK/cdk7 functions as a master cell cycle regulator by phosphorylating cyclin-dependent kinases for cell cycle progression. We have previously reported that protein kinase C-ι (PKC-ι) associates with CAK/cdk7. In this investigation, immunofluorescence confocal microscopy was used to provide further evidence for the co-localization of PKC-ι with CAK/cdk7. PKC-ι was labeled with Alexa Fluor 488 (green fluorescent dye) and CAK/cdk7 was labeled with Alexa Fluor 555 (red fluorescent dye). The fusion of the red and green fluorescent colors produced a yellow color, which was used to quantify co-localization of PKC-ι and CAK/cdk7. Confocal microscopy revealed the co-localization of PKC-ι with CAK/cdk7 in both the cytoplasm and nucleus of U-373 MG cells