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Related Experiment Videos

Estrogen receptor pathways to AP-1.

P J Kushner1, D A Agard, G L Greene

  • 1Metabolic Research Unit, 1119 HSW, University of California, 3rd and Parnassus, 94143-0540, San Francisco, CA, USA. kushner@itsa.ucsf.edu

The Journal of Steroid Biochemistry and Molecular Biology
|February 13, 2001
PubMed
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Estrogen receptor (ER) action at AP-1 sites involves two distinct mechanisms. ERalpha ligands activate coactivators, while SERMs with ERbeta or truncated ERalpha release repressors.

Area of Science:

  • Molecular Biology
  • Endocrinology
  • Gene Regulation

Background:

  • Estrogen receptor (ER) regulates gene transcription by binding to estrogen response elements and recruiting coactivator complexes like CBP-p160.
  • ER also influences transcription at AP-1 sites, which bind Jun/Fos transcription factors, but the mechanisms are less understood.

Purpose of the Study:

  • To review and propose mechanisms by which ER modulates the activity of Jun/Fos transcription factors.
  • To differentiate ER action pathways based on ER subtype (ERalpha vs. ERbeta) and ligand type (estrogen vs. SERMs).

Main Methods:

  • Review of existing evidence on ER interactions with AP-1 sites and associated protein complexes.
  • Proposal of mechanistic models for ERalpha and ERbeta/SERM actions at AP-1 sites.

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Main Results:

  • Estrogen-bound ERalpha complexes utilize activation functions (AF-1, AF-2) to enhance coactivator activity within the Jun/Fos complex.
  • Selective estrogen receptor modulators (SERMs) complexed with ERbeta or truncated ERalpha derivatives use their DNA binding domain to displace histone deacetylase (HDAC) repressors from the Jun/Fos coactivator complex.

Conclusions:

  • ER exerts distinct regulatory effects on Jun/Fos activity through at least two different molecular mechanisms.
  • These mechanisms depend on the specific ER subtype and the nature of the ligand, suggesting complex physiological roles for ER at AP-1 sites.