Opposite effects of alternative TZF spliced variants on androgen receptor

Biochem Biophys Res Commun. 2006 Mar 10;341(2):515-21. doi: 10.1016/j.bbrc.2005.12.213. Epub 2006 Jan 13.


We previously demonstrated that testicular zinc-finger protein (TZF) was a corepressor of the androgen receptor (AR). In the present study, we further showed that TZF-L, an alternative spliced variant of TZF, enhanced transactivation function of AR. Deletion analysis of TZF-L revealed that its N-terminus, which almost corresponded to that of TZF, but not its C-terminus was able to interact with AR. Additional analysis suggested that TZF and TZF-L were able to form both homodimers and heterodimers. TZF-L inhibited the homodimer formation of TZF and the intranuclear dot formation of TZF. We propose that in the unique regulation system of AR-mediated transactivation, two spliced isoforms of TZF act as coactivator and corepressor, respectively.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Alternative Splicing*
  • Amino Acid Motifs
  • Animals
  • COS Cells
  • Cell Line, Tumor
  • Chlorocebus aethiops
  • Dimerization
  • Gene Deletion
  • Genes, Reporter
  • Humans
  • Immunoblotting
  • Immunoprecipitation
  • Mice
  • Microscopy, Confocal
  • Models, Biological
  • NIH 3T3 Cells
  • Plasmids / metabolism
  • Protein Isoforms
  • Protein Structure, Tertiary
  • Receptors, Androgen / metabolism*
  • Repressor Proteins / chemistry
  • Repressor Proteins / metabolism*
  • Transcriptional Activation
  • Transfection


  • Protein Isoforms
  • Receptors, Androgen
  • Repressor Proteins
  • Rog protein, mouse
  • ZBTB32 protein, human