It is well known that protein kinase C (PKC) shows different translocation depending on subtype and stimulation, contributing to the physiological importance of the enzyme. However, molecular mechanism causing the different translocation has been unknown. Therefore, using GFP-tagged mutant epsilon PKC, we attempted to identify the intramolecular domains required for saturated fatty acid-induced translocation of epsilon PKC to the plasma membrane, and compared with those necessary for unsaturated fatty acid-induced translocation to the Golgi complex. We found that, unlike in the case of unsaturated fatty-acid induced translocation, both Cl B domain and pseudosubstrate region are necessary for the saturated fatty acid-induced translocation of epsilon PKC to the plasma membrane. The results suggest that different domains of PKC mediate distinct translocation depending on different stimulations, contributing to their subtype- and stimulation-specific functions. (C) 2013 Elsevier Inc. All rights reserved.