Inhibition of Estrogen Receptor Action by the Orphan Receptors, SHP and DAX-1

Abstract

The estrogen receptor is a critical diagnostic marker and therapeutic target for a large number of breast cancers. In support of DoD grant # DAMD17-99-1-9163, we present our findings regarding the mechanisms by which two orphan nuclear receptors, SHP and DAX-1 inhibit the actions of ER-alpha and ER-beta action. Consistent with prior studies of Shp, we show that Dax-1 binds directly to ER-a and ER-beta in an agonist dependent manner. Additionally, our data suggest that this interaction is sufficient to disrupt transcriptional activation of estrogen responsive reporters by ER-alpha and ER-beta in a dose dependent manner. Mutational analysis revealed that a 90 amino acid region of DAX-1 was sufficient to interact with agonist bound ER-alpha and ER-beta. This region contains two LXXML motifs similar to the LXXLL motifs found in ligand-dependent co-activators of the SRC-1 family. Consistent with this, a peptide containing LHRLL from the second NR Box of GRIP-1 was able to compete away the interaction between ER-alpha and this 90 amino acid fragment. Therefore, the mechanism by which DAX-1 interacts with ER-alpha and ER-beta is similar to the interaction of agonist bound ER and the SRC-1 family of nuclear receptor co-activators. Additionally, over-expression of SRC-1 was sufficient to override DAX-1-mediated repression of ER activity.

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Document Details

Document Type
Technical Report
Publication Date
Dec 01, 2003
Accession Number
ADA419517

Entities

People

  • James Direnzo

Organizations

  • Dartmouth College

Tags

DTIC Thesaurus Topics

  • Abstracts
  • Acids
  • Amino Acids
  • Biomedical Research
  • Breast Cancer
  • Cell Line
  • Cells
  • Elements
  • Estrogens
  • Genetic Structures
  • Hormones
  • Hybrid Systems
  • Inhibition
  • Medical Personnel
  • Neoplasms
  • Proteins
  • Thyroid Hormones

Fields of Study

  • Biology

Readers

  • Breast cancer cell signaling and growth regulation.