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Insulin potentiates the transactivation potency of the glucocorticoid receptor
Author(s) -
Georgakopoulos A.,
Tsawdaroglou N.
Publication year - 1996
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(96)00115-9
Subject(s) - transactivation , glucocorticoid receptor , glucocorticoid , hormone response element , insulin , phosphorylation , nuclear receptor , chemistry , insulin receptor , potency , endocrinology , medicine , biology , biochemistry , in vitro , insulin resistance , transcription factor , gene , cancer , estrogen receptor , breast cancer
A single copy of a glucocorticoid‐responsive element (GRE) is sufficient in mediating the combinatorial response of a promoter to both glucocorticoids and insulin in HepG2 cells. This requires the presence of active glucocorticoid receptor (GR) since the response is significantly inhibited by the anti‐glucocorticoid RU30406. The N′‐ and C′‐terminal parts of the GR protein are not involved in mediating the response. Insulin had no effect on GR binding to GRE but it affected both the level and the phosphorylation state of nuclear‐bound GR. Thus, insulin alters the GR transactivation potency while, concomitantly, modifies the molecule at the posttranslational level.