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J Biol Chem, Vol. 273, Issue 17, 10755-10762, April 24, 1998

Visualization of Dynamic Trafficking of a Protein Kinase C II/Green Fluorescent Protein Conjugate Reveals Differences in G Protein-coupled Receptor Activation and Desensitization

Xiao Feng, Jie Zhang^§, Larry S. Barak^§, Tobias Meyer, Marc G. Caron^§¶, and Yusuf A. Hannun^¶

From the Departments of  Cell Biology and ^¶ Medicine, ^§ Howard Hughes Medical Institute Laboratories, Duke University Medical Center, Durham, North Carolina 27710

Protein kinase C (PKC) links various extracellular signals to intracellular responses and is activated by diverse intracellular factors including diacylglycerol, Ca²⁺, and arachidonic acid. In this study, using a fully functional green fluorescent protein conjugated PKCII (GFP-PKCII), we demonstrate a novel approach to study the dynamic redistribution of PKC in live cells in response to G protein-coupled receptor activation. Agonist-induced PKC translocation was rapid, transient, and selectively mediated by the activation of G_q- but not G_s- or G_i-coupled receptors. Interestingly, although the stimuli were continuously present, only one brief peak of PKC membrane translocation was observed, consistent with rapid desensitization of the signaling pathway. Moreover, when GFP-PKCII was used to examine cross-talk between two G_q-coupled receptors, angiotensin II type 1A receptor (AT_1AR) and endothelin A receptor (ET_AR), activation of ET_ARs resulted in a subsequent loss of AT_1AR responsiveness, whereas stimulation of AT_1ARs did not cause desensitization of the ET_AR signaling. The development of GFP-PKCII has allowed not only the real time visualization of the dynamic PKC trafficking in live cells in response to physiological stimuli but has also provided a direct and sensitive means in the assessment of activation and desensitization of receptors implicated in the phospholipase C signaling pathway.

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