The glucocorticoid receptor synergizes with Jun homodimers to activate AP-1-regulated promoters lacking GR binding sites

Chem Senses. 1995 Apr;20(2):251-5. doi: 10.1093/chemse/20.2.251.

Abstract

Jun/Fos (AP-1) and steroid hormone receptors (SHR) are distinct families of transcription factors that convert extracellular signals into long-term genetic responses. Despite clear differences in their modes of activation and DNA binding specificities, a regulatory cross-talk between AP-1 and SHR such as the glucocorticoid receptor (GR), has been established. Here, we show that the hormone-activated GR negatively or positively modulates the expression of AP-1-dependent genes, depending on the subunits of the dimeric AP-1 complex. This type of regulation does not depend on the presence of a GR binding site in the promoter and is mediated through the DNA binding domain of Jun. Since individual subunits of AP-1 exhibit small differences in sequence specificity, specific subsets of AP-1-dependent genes may be regulated by steroid hormones in different directions.

Publication types

  • Research Support, Non-U.S. Gov't
  • Review

MeSH terms

  • Animals
  • Binding Sites
  • DNA / genetics
  • DNA / metabolism
  • Drug Synergism
  • Gene Expression Regulation / physiology*
  • Humans
  • Mice
  • Oncogene Protein p65(gag-jun) / metabolism
  • Oncogene Protein p65(gag-jun) / physiology*
  • Oncogene Proteins v-fos / metabolism
  • Oncogene Proteins v-fos / physiology*
  • Promoter Regions, Genetic / physiology*
  • Receptors, Glucocorticoid / metabolism
  • Receptors, Glucocorticoid / physiology*
  • Transcription Factor AP-1 / physiology*
  • Transcriptional Activation

Substances

  • Oncogene Protein p65(gag-jun)
  • Oncogene Proteins v-fos
  • Receptors, Glucocorticoid
  • Transcription Factor AP-1
  • DNA