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J Biol Chem, Vol. 275, Issue 10, 7158-7166, March 10, 2000

Truncated Estrogen Receptor Product-1 Suppresses Estrogen Receptor Transactivation by Dimerization with Estrogen Receptors alpha  and beta *

Eileen M. ResnickDagger , Derek A. Schreihofer§, Ammasi Periasamy, and Margaret A. Shupnik§||

From the Departments of Dagger  Pharmacology, § Internal Medicine, and  Biology, University of Virginia, Charlottesville, Virginia 22903

The estrogen receptor (ER) is a ligand-activated transcription factor that acts as a homodimer. Truncated estrogen receptor product-1 (TERP-1) is a pituitary-specific, estrogen-induced, isoform of rat ERalpha that is transcribed from a unique start site and contains only the C-terminal region of the full-length receptor. TERP-1 does not affect transcription directly but suppresses ligand-activated ERalpha and ERbeta activity. Because TERP-1 contains a dimerization domain and part of the coactivator binding pocket, we hypothesized that it modulates ER function by direct interactions with full-length ER or the steroid receptor coactivator, SRC-1. Localization studies demonstrate that TERP-1 is present in the cytoplasm and nucleus of transfected cells and colocalizes with nuclear ER. Protein binding studies show that TERP-1 forms heterodimers with both ERalpha and ERbeta and inhibits ERalpha binding to its cognate DNA response element. TERP-1 also binds SRC-1, and increasing levels of SRC-1 decrease the TERP-1-ERalpha interactions, in agreement with the rescue of TERP-1-suppressed ERalpha transcriptional activity by SRC-1. Mutational analysis of TERP-1 and ERalpha in the activation helix and the AF-2 dimerization helix indicates that TERP-1 acts predominantly through dimerization with ERalpha . Therefore, TERP-1 suppression of ER transcription occurs primarily by formation of inactive heterodimers and secondarily by competition for coactivators.

* This work was supported by National Institutes of Health Grant R01 HD25719/DK57082 (to M. A. S.) and funds from the Lalor Foundation (to D. A. S.). This work was also supported by NICHD, National Institutes of Health Grant U54 HD28934 through a cooperative agreement as part of the Specialized Cooperative Centers Program in Reproductive Research.The costs of publication of this article were defrayed in part by the payment of page charges. The article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

|| To whom correspondence should be addressed: Box 578 HSC, University of Virginia, Charlottesville, VA 22908. Tel.: 804-982-0010; Fax: 804-982-0088; E-mail: mas3x@virginia.edu.

Copyright © 2000 by The American Society for Biochemistry and Molecular Biology, Inc.
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