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    Biochem Biophys Res Commun. 2006 Mar 10;341(2):515-21. Epub 2006 Jan 13.

    Opposite effects of alternative TZF spliced variants on androgen receptor.

    Tao RH, Kawate H, Ohnaka K, Ishizuka M, Hagiwara H, Takayanagi R.

    Department of Geriatric Medicine, Graduate School of Medical Sciences, Kyushu University, Maidashi 3-1-1, Higashi-ku, Fukuoka 812-8582, Japan.

    We previously demonstrated that testicular zinc-finger protein (TZF) was a corepressor of the androgen receptor (AR). In the present study, we further showed that TZF-L, an alternative spliced variant of TZF, enhanced transactivation function of AR. Deletion analysis of TZF-L revealed that its N-terminus, which almost corresponded to that of TZF, but not its C-terminus was able to interact with AR. Additional analysis suggested that TZF and TZF-L were able to form both homodimers and heterodimers. TZF-L inhibited the homodimer formation of TZF and the intranuclear dot formation of TZF. We propose that in the unique regulation system of AR-mediated transactivation, two spliced isoforms of TZF act as coactivator and corepressor, respectively.

    PMID: 16446156 [PubMed - indexed for MEDLINE]

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