Testicular zinc finger protein recruits histone deacetylase 2 and suppresses the transactivation function and intranuclear foci formation of agonist-bound androgen receptor competitively with TIF2

Rong Hua Tao, Hisaya Kawate, Yin Wu, Keizo Ohnaka, Masamichi Ishizuka, Atsuto Inoue, Hiromi Hagiwara, Ryoichi Takayanagi

研究成果: Contribution to journalArticle査読

16 被引用数 (Scopus)

抄録

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.

本文言語英語
ページ(範囲)150-165
ページ数16
ジャーナルMolecular and Cellular Endocrinology
247
1-2
DOI
出版ステータス出版済み - 3 9 2006

All Science Journal Classification (ASJC) codes

  • 生化学
  • 分子生物学
  • 内分泌学

フィンガープリント

「Testicular zinc finger protein recruits histone deacetylase 2 and suppresses the transactivation function and intranuclear foci formation of agonist-bound androgen receptor competitively with TIF2」の研究トピックを掘り下げます。これらがまとまってユニークなフィンガープリントを構成します。

引用スタイル