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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.
MedLine Citation:
PMID:  23353652     Owner:  NLM     Status:  Publisher    
Abstract/OtherAbstract:
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, contibuting to their subtype- and stimulation-specific functions.
Authors:
Takaaki Nishimoto; Kaori Kashiwagi; Naoaki Saito; Yasuhito Shirai
Publication Detail:
Type:  JOURNAL ARTICLE     Date:  2013-1-24
Journal Detail:
Title:  Biochemical and biophysical research communications     Volume:  -     ISSN:  1090-2104     ISO Abbreviation:  Biochem. Biophys. Res. Commun.     Publication Date:  2013 Jan 
Date Detail:
Created Date:  2013-1-28     Completed Date:  -     Revised Date:  -    
Medline Journal Info:
Nlm Unique ID:  0372516     Medline TA:  Biochem Biophys Res Commun     Country:  -    
Other Details:
Languages:  ENG     Pagination:  -     Citation Subset:  -    
Copyright Information:
Copyright © 2013 Elsevier Inc. All rights reserved.
Affiliation:
The Laboratory of molecular pharmacology, Biosignal Research Center.
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