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This version published online on January 6, 2005
Molecular Endocrinology, doi:10.1210/me.2004-0326
A more recent version of this article appeared on April 1, 2005
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Submitted on August 19, 2004
Accepted on December 23, 2004

ANALYSIS OF ESTROGEN RECEPTOR {alpha}-Sp1 INTERACTIONS IN BREAST CANCER CELLS BY FLUORESCENCE RESONANCE ENERGY TRANSFER

Kyounghyun Kim, Rola Barhoumi, Robert Burghardt, and Stephen Safe*

Department of Veterinary Physiology and Pharmacology; Department of Veterinary Anatomy and Public Health, Texas A&M University, College Station, TX 77843 and Institute of Biosciences and Technology, Texas A&M University System Health Science Center, Houston, TX 77030-3303

* To whom correspondence should be addressed. E-mail: ssafe{at}cvm.tamu.edu.

Estrogen-dependent regulation of several genes associated with cell cycle progression, proliferation and nucleotide metabolism in breast cancer cells is associated with interactions of estrogen receptor {alpha} (ER{alpha})/Sp1 with GC-rich promoter elements. This study investigates ligand-dependent interactions of ER{alpha} and Sp1 in MCF-7 breast cancer cells using fluorescence resonance energy transfer (FRET). Chimeric ER{alpha} and Sp1 proteins fused to cyan fluorescent protein (CFP) or yellow fluorescent protein (YFP) were transfected into MCF-7 cells and a FRET signal was induced after treatment with 17{beta}-estradiol, 4'-hydroxytamoxifen or ICI 182,780. Induction of FRET by these ER{alpha} agonists/antagonists was paralleled by their activation of gene expression in cells transfected with a construct (pSp13) containing three tandem Sp1 binding sites linked to a luciferase reporter gene. In contrast, interactions between ER{alpha} and Sp1{Delta}DBD (a DBD deletion mutant of Sp1) are not observed, and this is consistent with the critical role of the C-terminal DBD of Sp1 for interaction with ER{alpha}. Results of the FRET assay are consistent with in vitro studies on ER{alpha}/Sp1 interactions and transactivation, and confirm that ER{alpha} and Sp1 interact in living breast cancer cells.
Key words: FRET • ER{alpha}/Sp1 • interactions

NURSA Molecule Pages Link:

Nuclear Receptors:   ERα
Ligands:   17β-Estradiol  |  4-Hydroxytamoxifen



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