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Protein kinase C (PKC) changes its subcellular localization depending on extracellular signals including hormones and neurotransmitters. Such translocation is referred to as "targeting" in this review. The live imaging technique using GFP has allowed the dynamic movement of PKC to be visualized in living cells and revealed a remarkable diversity in PKC targeting. These studies indicate an importance of targeting in regulating the physiological and isotype-specific function of PKC. Like PKC, diacylglycerol kinase (DGK), which phosphorylates diacylglycerol resulting in attenuation of PKC, subtype-specifically translocates to particular subcellular compartments including the plasma membrane and Golgi complex. In addition, it has been shown that the localization and activation of the two functionally-related kinases are well organized by direct interaction and phosphorylation. This review summarizes diversity in targeting of PKC and DGK and the molecular mechanisms regulating their targeting.

Analysis of molecular mechanism regulating spatio-temporal localization and activity of protein kinase C and diacylglycerol kinase using live imaging.