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DJ-1 positively regulates the androgen receptor by impairing the binding of PIASx alpha to the receptor.

DJ-1 was first identified as a novel candidate of the oncogene product that transformed mouse NIH3T3 cells in cooperation with an activated ras. Later DJ-1 was also found to be an infertility-related protein that was reduced in rat sperm treated with sperm toxicants that cause infertility in rats. To determine the functions of DJ-1, cDNAs encoding DJ-1-binding proteins were screened by the yeast two-hybrid method. Of several proteins identified, PIASx alpha/ARIP3, a modulator of androgen receptor (AR), was first characterized as the DJ-1-binding protein in this study. DJ-1 directly bound to the AR-binding region of PIASx alpha by an in vitro coimmunoprecipitation assay and also bound to PIASx alpha in human 293T cells. Both proteins were co-localized in the nuclei. PIASx alpha inhibited the AR transcription activity in a dose-dependent manner in cotransfected monkey CV1 cells with an androgen responsive element-luciferase reporter. Introduction of DJ-1 into CV1 cells in a state of inhibition of AR activity by PIASx alpha restored AR transcription activity by absorbing PIASx alpha from the AR-PIASx alpha complex, while a DJ-1 mutant harboring an amino acid substitution at number 130 from lysine to arginine did not restore it. These results indicate that DJ-1 is a positive regulator of the androgen receptor.

Pubmed ID: 11477070


  • Takahashi K
  • Taira T
  • Niki T
  • Seino C
  • Iguchi-Ariga SM
  • Ariga H


The Journal of biological chemistry

Publication Data

October 5, 2001

Associated Grants


Mesh Terms

  • 3T3 Cells
  • Animals
  • Cells, Cultured
  • Gene Silencing
  • Haplorhini
  • Humans
  • Intracellular Signaling Peptides and Proteins
  • Mice
  • Oncogene Proteins
  • Protein Inhibitors of Activated STAT
  • Proteins
  • Receptors, Androgen
  • Transcription, Genetic
  • Tumor Cells, Cultured