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Rho GDP dissociation inhibitor alpha interacts with estrogen receptor alpha and influences estrogen responsiveness

Academic Article
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Overview

authors

  • El Marzouk, S.
  • Schultz-Norton, J. R.
  • Likhite, V. S.
  • McLeod, I. X.
  • Yates III, John
  • Nardulli, A. M.

publication date

  • September 2007

journal

  • Journal of Molecular Endocrinology  Journal

abstract

  • Estrogen receptor alpha (ER alpha) is a ligand-activated transcription factor that regulates expression of estrogen-responsive genes. Upon binding of the ligand-occupied ER alpha to estrogen response elements (EREs) in DNA, the receptor interacts with a variety of coregulatory proteins to modulate transcription of target genes. We have isolated and identified a number of proteins associated with the DNA-bound ER alpha. One of these proteins, Rho guanosine diphosphate (GDP) dissociation inhibitor alpha (RhoGDI alpha), is a negative regulator of the Rho family of GTP-binding proteins. In this study, we demonstrate that endogenously expressed RhoGDI alpha is present in the nucleus as well as the cytoplasm of MCF-7 breast cancer cells, and that RhoGDI alpha binds directly to ER alpha, alters the ER alpha-ERE interaction, and influences the ability of ER alpha to regulate transcription of a heterologous estrogen-responsive reporter plasmid in transient transfection assays as well as endogenous, estrogen-responsive genes in MCF-7 cells. Our studies suggest that, in addition to the activity of RhoGDI alpha in the cytoplasm, it also influences ER alpha signaling in the nucleus.

subject areas

  • Cell Nucleus
  • Cytoplasm
  • Estrogen Receptor alpha
  • Estrogens
  • Gene Expression Regulation
  • Guanine Nucleotide Dissociation Inhibitors
  • HeLa Cells
  • Humans
  • Protein Binding
  • Response Elements
  • Tissue Distribution
  • Tumor Cells, Cultured
  • rho Guanine Nucleotide Dissociation Inhibitor alpha
  • rho-Specific Guanine Nucleotide Dissociation Inhibitors
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Identity

International Standard Serial Number (ISSN)

  • 0952-5041

Digital Object Identifier (DOI)

  • 10.1677/jme-07-0055

PubMed ID

  • 17909265
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Additional Document Info

start page

  • 249

end page

  • 259

volume

  • 39

issue

  • 3-4

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