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J Biol Chem, Vol. 274, Issue 15, 10363-10371, April 9, 1999

Redox-dependent Regulation of Nuclear Import of the Glucocorticoid Receptor

Kensaku Okamoto, Hirotoshi Tanaka, Hidesato Ogawa^¶, Yuichi Makino, Hidetaka Eguchi, Shin-ichi Hayashi, Noritada Yoshikawa, Lorenz Poellinger^**, Kazuhiko Umesono^¶, and Isao Makino

From the  Second Department of Internal Medicine, Asahikawa Medical College, Nishikagura, Asahikawa 078-8510, the ^¶ Department of Genetics and Molecular Biology, Institute for Virus Research, Kyoto University, Shogoin, Kawahara-cho, Kyoto 606-8507, the  Department of Biochemistry, Saitama Cancer Center Research Institute, Ina, Saitama 362-0800, Japan, and the ^** Department of Cell and Molecular Biology, Medical Nobel Institute, Karolinska Institutet, Stockholm S-171 77, Sweden

A number of transcription factors including the glucocorticoid receptor (GR) are regulated in a redox-dependent fashion. We have previously reported that the functional activity of the GR is suppressed under oxidative conditions and restored in the presence of reducing reagents. In the present study, we have used a chimeric human GR fused to the Aequorea green fluorescent protein and demonstrated that both ligand-dependent and -independent nuclear translocation of the GR is impaired under oxidative conditions in living cells. Substitution of Cys-481 for Ser within NL1 of the human GR resulted in reduction of sensitivity to oxidative treatment, strongly indicating that Cys-481 is one of the target amino acids for redox regulation of the receptor. Taken together, we may conclude that redox-dependent regulation of nuclear translocation of the GR constitutes an important mechanism for modulation of glucocorticoid-dependent signal transduction.

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