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Originally published In Press as doi:10.1074/jbc.M203423200 on May 6, 2002

J. Biol. Chem., Vol. 277, Issue 29, 25904-25913, July 19, 2002
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Tip60 and Histone Deacetylase 1 Regulate Androgen Receptor Activity through Changes to the Acetylation Status of the Receptor*

Luke Gaughan, Ian R. Logan, Susan Cook, David E. Neal, and Craig N. RobsonDagger

From the Prostate Research Group, School of Surgical Sciences, University of Newcastle Upon Tyne, Medical School, Framlington Place, Newcastle Upon Tyne NE2 4HH, United Kingdom

The androgen receptor (AR), a member of the nuclear hormone receptor superfamily, is thought to play an important role in the development of prostate cancer. The AR is a hormone-dependent transcription factor that activates expression of numerous androgen-responsive genes. Histone acetyltransferase-containing proteins have been shown to increase activity of several transcription factors, including nuclear hormone receptors, by eliciting histone acetylation, which facilitates promoter access to the transcriptional machinery. Conversely, histone deacetylases (HDACs) have been identified which reduce levels of histone acetylation and are associated with transcriptional repression by various transcription factors. We have previously shown that Tip60 (Tat-interactive protein, 60 kDa) is a bona fide co-activator protein for the AR. Here we show that Tip60 directly acetylates the AR, which we demonstrate is a requisite for Tip60-mediated transcription. To define a mechanism for repression of AR function, we demonstrate that AR activity is specifically down-regulated by the histone deacetylase activity of HDAC1. Furthermore, using both mammalian two-hybrid and immunoprecipitation experiments, we show that AR and HDAC1 interact, suggestive of a direct role for down-regulation of AR activity by HDAC1. In chromatin immunoprecipitation assays, we provide evidence that AR, Tip60, and HDAC1 form a trimeric complex upon the endogenous AR-responsive PSA promoter, suggesting that acetylation and deacetylation of the AR is an important mechanism for regulating transcriptional activity.

* This work was supported by the University of Newcastle Upon Tyne and the Association for International Cancer Research.The costs of publication of this article were defrayed in part by the payment of page charges. The article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

Dagger To whom all correspondence should be addressed. Tel.: 44-191-222-7076; Fax: 44-191-222-8514; E-mail: c.n.robson@ncl.ac.uk.

Copyright © 2002 by The American Society for Biochemistry and Molecular Biology, Inc.


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