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A novel estrogen receptor alpha-associated protein, template-activating factor I beta, inhibits acetylation and transactivation

Academic Article
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Overview

authors

  • Loven, M. A.
  • Muster, N.
  • Yates III, John
  • Nardulli, A. M.

publication date

  • January 2003

journal

  • Molecular Endocrinology  Journal

abstract

  • Estrogen receptor-alpha (ERalpha) functions as a ligand-activated transcription factor that alters expression of estrogen-responsive genes in target cells. Numerous regulatory proteins interact with ERalpha to influence estrogen-mediated transactivation. We have identified a novel coregulatory protein, template-activating factor-Ibeta (TAF-Ibeta), which binds to ERalpha in vitro when the receptor is not complexed with an estrogen response element. The central region of TAF-Ibeta interacts with both the DNA-binding domain and the carboxy-terminal region of ERalpha. Coimmunoprecipitation experiments demonstrate that TAF-Ibeta is associated with the unoccupied, but not the estrogen-occupied, ERalpha in MCF-7 breast cancer cells. Overexpression of TAF-Ibeta inhibits ERalpha-mediated transcription in a dose- dependent manner. TAF-Ibeta represses p300-mediated acetylation of histones and ERalpha in vitro and decreases ERalpha acetylation in vivo. TAF-Ibeta also binds to other nuclear receptor superfamily members and represses thyroid hormone receptor beta- induced transcription in transient transfection assays. Taken together, these data provide evidence that TAF-Ibeta regulates transcription of estrogen- responsive genes by modulating acetylation of histones and ERalpha and that the effects of TAF-Ibeta extend to other nuclear receptor superfamily members as well.

subject areas

  • Acetylation
  • Breast Neoplasms
  • Chromosomal Proteins, Non-Histone
  • Dose-Response Relationship, Drug
  • Estrogen Receptor alpha
  • Gene Expression Regulation
  • Histone Chaperones
  • Humans
  • Osteosarcoma
  • Protein Structure, Tertiary
  • Receptors, Cytoplasmic and Nuclear
  • Receptors, Estrogen
  • Structure-Activity Relationship
  • Transcription Factors
  • Transcriptional Activation
  • Tumor Cells, Cultured
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Identity

International Standard Serial Number (ISSN)

  • 0888-8809

Digital Object Identifier (DOI)

  • 10.1210/me.2002-0280

PubMed ID

  • 12511607
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Additional Document Info

start page

  • 67

end page

  • 78

volume

  • 17

issue

  • 1

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