| First Author | Fan S | Year | 2006 |
| Journal | Biochem Biophys Res Commun | Volume | 341 |
| Issue | 1 | Pages | 192-201 |
| PubMed ID | 16414017 | Mgi Jnum | J:105325 |
| Mgi Id | MGI:3614729 | Doi | 10.1016/j.bbrc.2005.12.167 |
| Citation | Fan S, et al. (2006) Identification of the functional domains of ANT-1, a novel coactivator of the androgen receptor. Biochem Biophys Res Commun 341(1):192-201 |
| abstractText | 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. |
