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Submitted on February 21, 2007
Accepted on May 24, 2007
Department of Molecular and Cellular Biology, Baylor College of Medicine
* To whom correspondence should be addressed. E-mail: nweigel{at}bcm.tmc.edu.
Steroid receptors are hormone activated transcription factors whose expression and activities are also highly dependent upon post-translational modifications including phosphorylation. The remarkable number of phosphorylation sites in these receptors and the wide variety of kinases participating in their phosphorylation facilitates integration between cell signaling pathways and steroid receptor action. Sites have been identified in all of the functional domains although the sites are predominantly in the amino terminal portions of the receptors. Regulation of function is receptor specific, site specific, and often dependent upon activation of a specific cell signaling pathway. This complexity in part explains the early difficulties in identifying roles for phosphorylation in receptor function. With increased availability of phosphorylation site specific antibodies and better means to measure receptor activities, numerous roles for site specific phosphorylation have been identified including sensitivity of response to hormone, DNA binding, expression, stability, subcellular localization, and protein/protein interactions which determine the level of regulation of specific target genes. This review summarizes current knowledge regarding receptor phosphorylation and regulation of function. As functional assays become more sophisticated, it is likely that additional roles for phosphorylation in receptor function will be identified.
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