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

Research output: Contribution to journalArticle

14 Citations (Scopus)

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 languageEnglish
Pages (from-to)150-165
Number of pages16
JournalMolecular and Cellular Endocrinology
Volume247
Issue number1-2
DOIs
Publication statusPublished - Mar 9 2006

All Science Journal Classification (ASJC) codes

  • Biochemistry
  • Molecular Biology
  • Endocrinology

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