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¹ Laboratory of Molecular Pharmacology, Biosignal Research Center, Kobe University, 1-1 Rokkodai-cho, Nadaku, Kobe 657-8501, Japan
² Department of Clinical Pharmacy, Kobe Pharmaceutical University, Kobe 658-8558, Japan
³ Department of Molecular and Pharmacological Neuroscience, Graduate School of Biomedical Sciences, Hiroshima University, Hiroshima 734-8551, Japan
⁴ Department of Immunology and Oncology, National Center of Biotechnolog, CSIC, Campus de Cantoblanco, Madrid E-28049, Spain

Diacylglycerol kinase (DGK) has been suggested to be a pharmacological target of D--tocopherol for diabetic renal dysfunctions. However, the DGK subtypes involved in the D--tocopherol-induced improvement of diabetic renal dysfunctions and the activation mechanisms of DGK by D--tocopherol are still unknown. Therefore, using GFP-tagged DGK, ß, , and , we analyzed their response to D--tocopherol and its derivatives. Only DGK was translocated from the cytoplasm to the plasma membrane with elevation of kinase activity. In addition, troglitazone and trolox possessing ‘chroman ring’ similarly to D--tocopherol, induced the subtype-specific translocation of DGK. Furthermore, the translocation of DGK was abolished by pretreatment with tyrosine kinase inhibitors or by mutation on Tyr-334 of the kinase (YF mutant). D--tocopheryl succinate enhanced the Src-mediated tyrosine phosphorylation of wild-type DGK but the same reagent did not enhance that of the YF mutant. These results demonstrate that tyrosine phosphorylation on Tyr-334 and chroman ring are important for the D--tocopherol-induced translocation of DGK.

^* Correspondence: E-mail: shirai{at}kobe-u.ac.jp

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