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A more recent version of this article appeared on March 15, 2002
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M111975200v1
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Papers In Press, published online ahead of print January 4, 2002
J. Biol. Chem, 10.1074/jbc.M111975200
Submitted on December 15, 2001
Revised on January 2, 2002
Accepted on January 3, 2002

The FXXLF motif mediates androgen receptor-specific interactions with coregulators

Bin He, John T. Minges, Lori W. Lee, and Elizabeth M. Wilson

Department of Pediatrics and Biochemistry, University of North Carolina at Chapel Hill, Chapel Hill, NC 27599-7500

Corresponding Author: emw{at}med.unc.edu

The androgen receptor (AR) activation function 2 region of the ligand binding domain binds weakly the LXXLL motifs of p160 coactivators, engaging instead in an androgen dependent, interdomain interaction with an FXXLF motif in the AR NH2-terminus. Here we show that FXXLF motifs are present in previously reported AR coactivators ARA70/RFG, ARA55/Hic-5 and ARA54 that account for their selection in yeast two hybrid screens. Mammalian two hybrid assays, ligand dissociation rate studies and glutathione-S-transferase adsorption assays indicate androgen dependent selective interactions of these FXXLF motifs with the AR ligand binding domain. Mutagenesis of residues within activation function 2 indicates distinct but overlapping binding sites where specificity depends on sequence within and flanking the FXXLF motif. Mutagenesis of the FXXLF motifs eliminated interaction with the ligand binding domain but only modestly reduced AR coactivation in transcription assays. The studies indicate that the FXXLF binding motif is specific for the AR and mediates interactions both within the AR and with coregulatory proteins.


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