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Volume 272, Number 16, Issue of April 18, 1997 pp. 10457-10463
©1997 by The American Society for Biochemistry and Molecular Biology, Inc.

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Differential Phosphorylation of Chicken Progesterone Receptor in Hormone-dependent and Ligand-independent Activation

(Received for publication, January 16, 1997)

From the Department of Cell Biology, Baylor College of Medicine, Houston, Texas 77030

Many steroid receptors, including chicken progesterone receptor, have been shown to be activated in the absence of their cognate ligands by modulators of kinases and phosphatases. To investigate the molecular mechanism of ligand-independent activation, chicken progesterone receptor mutants in which either one or all four of the previously identified phosphorylation sites have been changed to nonphosphorylatable alanine were analyzed for their ability to be activated by progesterone, 8-bromoadenosine 3:5-cyclic monophosphate, or a dopamine agonist, SKF82958. Our current study shows that the receptor is differently phosphorylated in ligand-dependent and ligand-independent activation. The transcriptional activity of the receptor in response to 8-bromoadenosine 3:5-cyclic monophosphate is affected by mutation of either Ser²¹¹ or Ser²⁶⁰. In addition, our data demonstrated that none of the four sites is absolutely required for the activation of the receptor by either 8-bromoadenosine 3:5-cyclic monophosphate or the dopamine agonist. Treatment with 8-bromoadenosine 3:5-cyclic monophosphate did not increase the overall level of receptor phosphorylation or cause phosphorylation of the receptor at alternate sites. These data raise the possibility that ligand-independent activation of the chicken progesterone receptor may be mediated through changes in the phosphorylation of coregulators or other protein factors interacting with the receptors.

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