This Article Full Text Full Text (PDF) All Versions of this Article: 18/11/2649    most recent Author Manuscript (PDF) Purchase Article View Shopping Cart Alert me when this article is cited Alert me if a correction is posted Citation Map Services Email this article to a friend Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager NURSA Molecule Pages Link Request Copyright Permission Citing Articles Citing Articles via HighWire Citing Articles via Google Scholar Google Scholar Articles by Loven, M. A. Articles by Nardulli, A. M. Search for Related Content PubMed PubMed Citation Articles by Loven, M. A. Articles by Nardulli, A. M. Pubmed/NCBI databases Gene GEO Profiles HomoloGene UniGene Substance via MeSH

A Novel Estrogen Receptor -Associated Protein Alters Receptor-Deoxyribonucleic Acid Interactions and Represses Receptor-Mediated Transcription

Department of Molecular and Integrative Physiology (M.A.L., R.E.D., C.D.C., A.M.N.), University of Illinois, Urbana, Illinois 61801; Department of Biological Sciences (N.M.), University of California, Irvine, California 92697; and Department of Cell Biology (J.R.Y.), The Scripps Research Institute, La Jolla, California 92037

Address all correspondence and requests for reprints to: Ann M. Nardulli, Department of Molecular and Integrative Physiology, University of Illinois at Urbana-Champaign, 524 Burrill Hall, 407 South Goodwin Avenue, Urbana, Illinois 61801. E-mail: anardull{at}life.uiuc.edu.

Estrogen receptor (ER) serves as a ligand-activated transcription factor, turning on transcription of estrogen-responsive genes in target cells. Numerous regulatory proteins interact with the receptor to influence ER-mediated transactivation. In this study, we have identified pp32, which interacts with the DNA binding domain of ER when the receptor is free, but not when it is bound to an estrogen response element. Coimmunoprecipitation experiments demonstrate that endogenously expressed pp32 and ER from MCF-7 breast cancer cells interact. Although pp32 substantially enhances the association of the receptor with estrogen response element-containing DNA, overexpression of pp32 in MCF-7 cells decreases transcription of an estrogen-responsive reporter plasmid. pp32 Represses p300-mediated acetylation of ER and histones in vitro and inhibits acetylation of ER in vivo. pp32 Also binds to other nuclear receptors and inhibits thyroid hormone receptor ß-mediated transcription. Taken together, our studies provide evidence that pp32 plays a role in regulating transcription of estrogen-responsive genes by modulating acetylation of histones and ER and also influences transcription of other hormone-responsive genes as well.

NURSA Molecule Pages Link:

Nuclear Receptors:   TRβ  |  PPARγ  |  RXRα  |  ERα  |  PR

Coregulators:   pp32  |  p300

Ligands:   17β-Estradiol

This article has been cited by other articles:

				A. K. Rao, Y. S. Ziegler, I. X. McLeod, J. R. Yates, and A. M. Nardulli Effects of Cu/Zn Superoxide Dismutase on Estrogen Responsiveness and Oxidative Stress in Human Breast Cancer Cells Mol. Endocrinol., May 1, 2008; 22(5): 1113 - 1124. [Abstract] [Full Text] [PDF]

				C. D. Curtis, V. S. Likhite, I. X. McLeod, J. R. Yates, and A. M. Nardulli Interaction of the Tumor Metastasis Suppressor Nonmetastatic Protein 23 Homologue H1 and Estrogen Receptor {alpha} Alters Estrogen-Responsive Gene Expression Cancer Res., November 1, 2007; 67(21): 10600 - 10607. [Abstract] [Full Text] [PDF]

				J. R. Schultz-Norton, V. A. Gabisi, Y. S. Ziegler, I. X. McLeod, J. R. Yates, and A. M. Nardulli Interaction of estrogen receptor {alpha} with proliferating cell nuclear antigen Nucleic Acids Res., August 1, 2007; 35(15): 5028 - 5038. [Abstract] [Full Text] [PDF]

				N. Heldring, A. Pike, S. Andersson, J. Matthews, G. Cheng, J. Hartman, M. Tujague, A. Strom, E. Treuter, M. Warner, et al. Estrogen Receptors: How Do They Signal and What Are Their Targets Physiol Rev, July 1, 2007; 87(3): 905 - 931. [Abstract] [Full Text] [PDF]

				J. R. Schultz-Norton, K. A. Walt, Y. S. Ziegler, I. X. McLeod, J. R. Yates, L. T. Raetzman, and A. M. Nardulli The Deoxyribonucleic Acid Repair Protein Flap Endonuclease-1 Modulates Estrogen-Responsive Gene Expression Mol. Endocrinol., July 1, 2007; 21(7): 1569 - 1580. [Abstract] [Full Text] [PDF]

				J. R. Schultz-Norton, W. H. McDonald, J. R. Yates, and A. M. Nardulli Protein Disulfide Isomerase Serves as a Molecular Chaperone to Maintain Estrogen Receptor {alpha} Structure and Function Mol. Endocrinol., September 1, 2006; 20(9): 1982 - 1995. [Abstract] [Full Text] [PDF]

				T. Macfarlan, J. B. Parker, K. Nagata, and D. Chakravarti Thanatos-Associated Protein 7 Associates with Template Activating Factor-I{beta} and Inhibits Histone Acetylation to Repress Transcription Mol. Endocrinol., February 1, 2006; 20(2): 335 - 347. [Abstract] [Full Text] [PDF]

				J. Huang, X. Li, C. A. Maguire, R. Hilf, R. A. Bambara, and M. Muyan Binding of Estrogen Receptor {beta} to Estrogen Response Element in Situ Is Independent of Estradiol and Impaired by Its Amino Terminus Mol. Endocrinol., November 1, 2005; 19(11): 2696 - 2712. [Abstract] [Full Text] [PDF]