ARA24/Ran enhances the androgen-dependent NH2- and COOH-terminal interaction of the androgen receptor

Biochem Biophys Res Commun. 2008 Aug 29;373(3):373-7. doi: 10.1016/j.bbrc.2008.06.024. Epub 2008 Jun 17.


The androgen receptor (AR) acts as an androgen-dependent transcription factor controlling the development of prostate tissue. Upon binding to androgen, AR undergoes a dynamic structural change leading to interaction between the NH(2)- and COOH-terminal regions of AR (N-C interaction). ARA24/Ran, which is a small GTPase, functions as an AR coactivator. Here, we report that ARA24/Ran enhances the N-C interaction of AR. The constitutively GTP- or GDP-bound form of ARA24/Ran repressed the AR N-C interaction. ARA24/Ran did not enhance the transcriptional activities of AR mutants that disrupt the N-C interaction. ARA24/Ran formed an endogenous protein complex with nuclear AR, but not cytoplasmic AR. Unlike SRC-1 with the positive activity for AR N-C interaction, ARA24/Ran did not enhance the transcriptional activity of the COOH-terminal domain-deleted AR mutant that is constitutively localized in the nucleus. These data demonstrate that ARA24/Ran increases AR transactivation by enhancing the AR N-C interaction in the nucleus.

MeSH terms

  • Androgens / metabolism*
  • Cell Line, Tumor
  • Cell Nucleus / metabolism
  • Cytoplasm / metabolism
  • Humans
  • Male
  • Mutation
  • Prostate / metabolism
  • Prostatic Neoplasms / metabolism
  • Receptors, Androgen / genetics
  • Receptors, Androgen / metabolism*
  • Transcription, Genetic
  • Transcriptional Activation
  • ran GTP-Binding Protein / genetics
  • ran GTP-Binding Protein / metabolism*


  • Androgens
  • RAN protein, human
  • Receptors, Androgen
  • ran GTP-Binding Protein