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J Biol Chem, Vol. 274, Issue 15, 10363-10371, April 9, 1999
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From the 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.
Second Department of Internal Medicine, Department of Biochemistry,
Copyright © 1999 by The American Society for Biochemistry and Molecular Biology, Inc.
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