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.
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.
The Laboratory of Molecular Pharmacology, Biosignal Research Center, Kobe University, Rokkodai-cho 1-1, Nada-ku, Kobe 657-8501, Japan.
Takaaki
T
Nishimoto
Kaori
K
Kashiwagi
Naoaki
N
Saito
Yasuhito
Y
Shirai
D000818:Animals; D019556:COS Cells; D002462:Cell Membrane / Q000201:enzymology*; D002522:Chlorocebus aethiops; D005227:Fatty Acids / Q000378:metabolism* / Q000494:pharmacology; D057809:HEK293 Cells; D006801:Humans; D011493:Protein Kinase C / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D017434:Protein Structure, Tertiary / Q000235:genetics; D021381:Protein Transport; D051381:Rats
D005227:Fatty Acids; D011493:Protein Kinase C