Abstract
We previously reported that testicular zinc finger protein (TZF) is a corepressor for androgen receptor (AR). The present study demonstrated that a central portion (amino acids 512-663) of TZF, TZF(512-663), is responsible for both binding to AR and repressing the transactivation. TZF recruited endogenous histone deacetylase 2 (HDAC2) and formed a complex with agonist-bound AR. Imaging analyses showed that TZF and TZF(512-663) were recruited by AR and simultaneously impaired distinct AR foci formation. Quantification of the foci number using a three-dimensional imaging method revealed that the number of intranuclear AR foci was related to its transactivation activity. Moreover, increased levels of TZF dissociated a coactivator, TIF2, from the AR foci and vice versa. These results indicate that the ligand-dependent transactivation function of AR is quantitatively related to its intranuclear foci formation, and suggest that corepressors, such as TZF, act on these intranuclear events competitively with coactivators.
Original language | English (US) |
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Pages (from-to) | 150-165 |
Number of pages | 16 |
Journal | Molecular and cellular endocrinology |
Volume | 247 |
Issue number | 1-2 |
DOIs | |
State | Published - Mar 9 2006 |
Externally published | Yes |
Keywords
- Androgen receptor
- Corepressor
- GFP
- HDAC
ASJC Scopus subject areas
- Biochemistry
- Molecular Biology
- Endocrinology