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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.

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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.

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