Nuclear protein kinase C and signal transduction.

Abstract

Protein kinase C (pKC) is a family of enzymes, consisting of ten isoenzymes. Some of the members of the pKC family are not dependent on calcium for their activity and also do not bind diacylglycerol. Protein kinase C is either translocated to the nucleus or present endogenously. Both calcium-dependent as well as calcium-independent isoenzymes are located in the nucleus. Protein kinase C has specific functions in the events activated within the nucleus during signal transduction. Three lines of approach have been taken to discern the nuclear function of pKC: pathways of activation of cytosolic pKC regulating nuclear events; translocation of pKC to the nucleus from the cytosol, and activation of native pKC in isolated nuclei. Protein kinase C contains a nuclear targeting bipartite motif and has a role in the nuclear calcium signaling process. Targeting and binding of pKC to the sites of replicational and posttranscriptional activity may be one of the mechanisms of the pKC signaling process. Protein kinase C-mediated activation of nuclear phosphatases and dephosphorylation of target nuclear proteins are the areas where much less attention has been paid. Exploring these avenues may lead to new insights into the molecular mechanism of nuclear signal transduction.