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A genetically‐encoded reporter reveals novel regulation of protein kinase D by calcium

The protein kinase D (PKD) family has been shown to play a role in many diverse cellular functions such as Golgi sorting, immune responses, apoptosis, cell growth and cell survival. We have generated a genetically‐encoded fluorescent reporter for PKD activity. Specifically, phosphorylation of the reporter expressed in mammalian cells causes changes in fluorescence resonance energy transfer (FRET) allowing real time imaging of phosphorylation by PKD. Importantly, pharmacological inhibition of PKD results in a reversal of the FRET change allowing one to visualize the dynamics of kinase and phosphatase activities. Using this reporter we are now exploring the mechanisms of PKD signaling downstream of endogenous G protein‐coupled receptors. In particular, we have identified a calcium component to PKD signaling. We are currently investigating the potential role of conventional PKC isoforms in the activation of PKD.