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Originally published In Press as doi:10.1074/jbc.M210744200 on December 31, 2002

J. Biol. Chem., Vol. 278, Issue 10, 8212-8218, March 7, 2003
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Dual Function of an Amino-terminal Amphipatic Helix in Androgen Receptor-mediated Transactivation through Specific and Nonspecific Response Elements*

Leen Callewaert, Guy VerrijdtDagger , Valerie Christiaens, Annemie HaelensDagger , and Frank Claessens§

From the Division of Biochemistry, Faculty of Medicine, Campus Gasthuisberg, University of Leuven, Herestraat 49, B-3000 Leuven, Belgium

Steroid receptors are transcription factors that, upon binding to their response elements, regulate the expression of several target genes via direct protein interactions with transcriptional coactivators. For the androgen receptor, additional interactions between the amino- and carboxyl-terminal regions have been reported. The first amino acids of the amino-terminal domain are necessary for this amino/carboxyl-terminal interaction. Deletion of a FQNLF core sequence in this region blunts the interaction, as does a G21E mutation. We investigated the effect of the aforementioned mutations in the context of the full size androgen receptor on a series of selective and nonselective androgen response elements. Strikingly, the FQNLF deletion strongly reduced the androgen receptor capacity to transactivate through nonselective motifs but did not affect its activity on selective elements. Although the G21E mutation strongly impairs the amino/carboxyl-terminal interaction, it does not significantly influence androgen receptor activity on either selective or nonselective elements. Surprisingly, this mutation leads to an increased binding of the amino-terminal domain to the glutamine-rich region of the steroid receptor coactivator-1 of the p160 family. Taken together, these data suggest that the amino-terminal amino acids of the androgen receptor play a key role in determining its transcriptional activity by modulating the interaction with the ligand-binding domain as well as interaction with p160 coactivators.

* This work was supported in part by the Geconcerteerde Onderzoeksactie van de Vlaamse Gemeenschap and by grants from the Fonds voor Wetenschappelijk Onderzoek, Vlaanderen.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 Recipient of a Postdoctoral Fellowship from the Fonds voor Wetenschappelijk Onderzoek-Vlaanderen.

§ To whom correspondence should be addressed. Tel.: 32-16-345770; Fax: 32-16-345995; E-mail: frank.claessens@med.kuleuven.ac.be.

Copyright © 2003 by The American Society for Biochemistry and Molecular Biology, Inc.
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