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Science 21 December 1990:
Vol. 250. no. 4988, pp. 1740 - 1743
DOI: 10.1126/science.2176746
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Articles

Science, Vol 250, Issue 4988, 1740-1743
Copyright © 1990 by American Association for the Advancement of Science

articles

Regulation of progesterone receptor-mediated transcription by phosphorylation

LA Denner, NL Weigel, BL Maxwell, WT Schrader, and BW O'Malley

Department of Cell Biology, Baylor College of Medicine, Houston, TX 77030.

The progesterone receptor (PR) in the chicken oviduct is a phosphoprotein that regulates gene transcription in the presence of progesterone. Treatment with progesterone in vivo stimulates phosphorylation of the progesterone receptor. With transient transfection assays, the present work has tested whether phosphorylation participates in the regulation of PR-mediated transcription. Treatment with 8-bromo-cyclic adenosine monophosphate (8-Br cAMP), a stimulator of cAMP-dependent protein kinase [protein kinase A (PKA)], mimicked progesterone-dependent, receptor-mediated transcription in the absence of progesterone. Inhibition of PKA blocked hormone action. Treatment with okadaic acid, an inhibitor of protein phosphatases 1 and 2A, stimulated transcription in a manner similar to that of progesterone. These observations suggest that phosphorylation of the PR or other proteins in the transcription complex can modulate PR-mediated transcription in vivo.


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