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

Shuli Fan, Kiminobu Goto, Guangchun Chen, Hidetaka Morinaga, Masatoshi Nomura, Taijiro Okabe, Hajime Nawata, Toshihiko Yanase

Research output: Contribution to journalArticlepeer-review

6 Citations (Scopus)


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.

Original languageEnglish
Pages (from-to)192-201
Number of pages10
JournalBiochemical and Biophysical Research Communications
Issue number1
Publication statusPublished - Mar 3 2006

All Science Journal Classification (ASJC) codes

  • Biophysics
  • Biochemistry
  • Molecular Biology
  • Cell Biology


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