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J. Biol. Chem., Vol. 276, Issue 27, 24806-24816, July 6, 2001

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Transactivation Specificity of Glucocorticoid Versus Progesterone Receptors
ROLE OF FUNCTIONALLY DIFFERENT INTERACTIONS OF TRANSCRIPTION FACTORS WITH AMINO- AND CARBOXYL-TERMINAL RECEPTOR DOMAINS^*

Liang-Nian Song, Barbara Huse^§, Sandro Rusconi^§, and S. Stoney Simons Jr.^¶

From the  Steroid Hormones Section, NIDDK/LMCB, National Institutes of Health, Bethesda, Maryland 20892 and ^§ Université de Fribourg Suisse, CH-1700 Fribourg, Switzerland

A major unanswered question of glucocorticoid and progesterone action is how different whole cell responses arise when both of the cognate receptors can bind to, and activate, the same hormone response elements. We have documented previously that the EC₅₀ of agonist complexes, and the partial agonist activity of antagonist complexes, of both glucocorticoid receptors (GRs) and progesterone receptors (PRs) are modulated by increased amounts of homologous receptor and of coregulators. We now ask whether these components can differentially alter GR and PR transcriptional properties. To remove possible cell-specific differences, we have examined both receptors in the common environment of a line of mouse mammary adenocarcinoma (1470.2) cells. In order to segregate the responses that might be due to unequal nucleosome reorganization by the two receptors from those reflecting interactions with other components, we chose a transiently transfected reporter containing a simple glucocorticoid response element (i.e. GREtkLUC). No significant differences are found with elevated levels of either receptor. However, major, qualitative differences are seen with the corepressors SMRT and NCoR, which afford opposite responses with GR and PR. Studies with chimeric GR/PR receptors indicate that no one segment of PR or GR is responsible for these properties and that the composite response likely involves interactions with both the amino and carboxyl termini of receptors. Collectively, the data suggest that GR and PR induction of responsive genes in a given cell can be differentially controlled, in part, by unequal interactions of multiple receptor domains with assorted nuclear cofactors.

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