Both C1B domain and pseudosubstrate region are necessary for saturated fatty acid-induced translocation of εPKC to the plasma membrane: distinct role of intramolecular domains for different translocation.
Biochemical and Biophysical Research Communications(2013)
Abstract
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 εPKC, we attempted to identify the intramolecular domains required for saturated fatty acid-induced translocation of εPKC 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 C1B domain and pseudosubstrate region are necessary for the saturated fatty acid-induced translocation of εPKC 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.
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Key words
Protein kinase C,Saturated fatty acid,Tridecanoic acid,Intramolecular domains,Mechanism of translocation
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