Identification of the functional domains of ANT-1, a novel coactivator of the androgen receptor

Biochem Biophys Res Commun. 2006 Mar 3;341(1):192-201. doi: 10.1016/j.bbrc.2005.12.167. Epub 2006 Jan 9.


Previously, we identified a transcriptional coactivator for the activation function-1 (AF-1) domain of the human androgen receptor (AR) and designated it androgen receptor N-terminal domain transactivating protein-1 (ANT-1). This coactivator, which contains multiple tetratricopeptide repeat (TPR) motifs from amino acid (aa) 294, is identical to a component of U5 small nuclear ribonucleoprotein particles and binds specifically to the AR or glucocorticoid receptor. Here, we identified four distinct functional domains. The AR-AF-1-binding domain, which bound to either aa 180-360 or 360-532 in AR-AF-1, clearly overlapped with TAU-1 and TAU-5. This domain and the subnuclear speckle formation domain in ANT-1 were assigned within the TPR motifs, while the transactivating and nuclear localization signal domains resided within the N-terminal sequence. The existence of these functional domains may further support the idea that ANT-1 can function as an AR-AF-1-specific coactivator while mediating a transcription-splicing coupling.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Adenine Nucleotide Translocator 1 / chemistry*
  • Adenine Nucleotide Translocator 1 / genetics
  • Adenine Nucleotide Translocator 1 / metabolism*
  • Amino Acid Substitution
  • Animals
  • Binding Sites
  • COS Cells
  • Chlorocebus aethiops
  • Mice
  • Mutagenesis, Site-Directed
  • NIH 3T3 Cells
  • Protein Binding
  • Protein Structure, Tertiary
  • Receptors, Androgen / chemistry*
  • Receptors, Androgen / metabolism*
  • Structure-Activity Relationship
  • Subcellular Fractions / metabolism*


  • Adenine Nucleotide Translocator 1
  • Receptors, Androgen