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.
journal_name
Mol Cell Endocrinoljournal_title
Molecular and cellular endocrinologyauthors
Tao RH,Kawate H,Wu Y,Ohnaka K,Ishizuka M,Inoue A,Hagiwara H,Takayanagi Rdoi
10.1016/j.mce.2005.12.052keywords:
subject
Has Abstractpub_date
2006-03-09 00:00:00pages
150-65issue
1-2eissn
0303-7207issn
1872-8057pii
S0303-7207(06)00003-7journal_volume
247pub_type
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