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Endocrinology Vol. 140, No. 12 5566-5578
Copyright © 1999 by The Endocrine Society

ARTICLES

The Estrogen Receptor ß-Isoform (ERß) of the Human Estrogen Receptor Modulates ER{alpha} Transcriptional Activity and Is a Key Regulator of the Cellular Response to Estrogens and Antiestrogens1

Julie M. Hall2 and Donald P. McDonnell

Department of Pharmacology and Cancer Biology, Duke University Medical Center, Durham, North Carolina 27710

Address all correspondence and requests for reprints to: Dr. Donald P. McDonnell, Department of Pharmacology and Cancer Biology, Duke University Medical Center, P.O. Box 3813, Durham, North Carolina 27710. E-mail: mcdon016{at}acpub.duke.edu

The human estrogen receptor {alpha} (ER{alpha}) and the recently identified ERß share a high degree of amino acid homology; however, there are significant differences in regions of these receptors that would be expected to influence transcriptional activity. Consequently, we compared the mechanism(s) by which these receptors regulate target gene transcription, and evaluated the cellular consequences of coexpression of both ER subtypes. Previously, it has been determined that ER{alpha} contains two distinct activation domains, ER{alpha}-AF-1 and ER{alpha}-AF-2, whose transcriptional activity is influenced by cell and promoter context. We determined that ERß, like ER{alpha}, contains a functional AF-2, however, the ERß-AF-2 domain functions independently within the receptor. Of additional significance was the finding that ERß does not contain a strong AF-1 within its amino-terminus but, rather, contains a repressor domain that when removed, increases the overall transcriptional activity of the receptor. The importance of these findings was revealed when it was determined that ERß functions as a transdominant inhibitor of ER{alpha} transcriptional activity at subsaturating hormone levels and that ERß decreases overall cellular sensitivity to estradiol. Additionally, the partial agonist activity of tamoxifen manifest through ER{alpha} in some contexts was completely abolished upon coexpression of ERß. In probing the mechanisms underlying ERß-mediated repression of ER{alpha} transcriptional activity we have determined that 1) ER{alpha} and ERß can form heterodimers within target cells; and 2) ERß interacts with target gene promoters in a ligand-independent manner. Cumulatively, these data indicate that one role of ERß is to modulate ER{alpha} transcriptional activity, and thus the relative expression level of the two isoforms will be a key determinant of cellular responses to agonists and antagonists.




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