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Published online April 9, 2007
doi:10.1083/jcb.200609178
The Journal of Cell Biology, Vol. 177, No. 1, 63-72
The Rockefeller University Press, 0021-9525 $30.00
© 2007 van Royen et al.
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Article

 Compartmentalization of androgen receptor protein–protein interactions in living cells

Martin E. van Royen1, Sónia M. Cunha1, Maartje C. Brink2, Karin A. Mattern1, Alex L. Nigg1, Hendrikus J. Dubbink1, Pernette J. Verschure2, Jan Trapman1, and Adriaan B. Houtsmuller1

1 Department of Pathology, Josephine Nefkens Institute, Erasmus MC, 3000 CA Rotterdam, Netherlands
2 Structure and Functional Organisation of the Cell Nucleus, Swammerdam Institute for Life Sciences, University of Amsterdam, 1090 GB Amsterdam, Netherlands

Correspondence to A.B. Houtsmuller: a.houtsmuller{at}erasmusmc.nl

Steroid receptors regulate gene expression in a ligand-dependent manner by binding specific DNA sequences. Ligand binding also changes the conformation of the ligand binding domain (LBD), allowing interaction with coregulators via LxxLL motifs. Androgen receptors (ARs) preferentially interact with coregulators containing LxxLL-related FxxLF motifs. The AR is regulated at an extra level by interaction of an FQNLF motif in the N-terminal domain with the C-terminal LBD (N/C interaction). Although it is generally recognized that AR coregulator and N/C interactions are essential for transcription regulation, their spatiotemporal organization is largely unknown. We performed simultaneous fluorescence resonance energy transfer and fluorescence redistribution after photobleaching measurements in living cells expressing ARs double tagged with yellow and cyan fluorescent proteins. We provide evidence that AR N/C interactions occur predominantly when ARs are mobile, possibly to prevent unfavorable or untimely cofactor interactions. N/C interactions are largely lost when AR transiently binds to DNA, predominantly in foci partly overlapping transcription sites. AR coregulator interactions occur preferentially when ARs are bound to DNA.

Abbreviations used in this paper: AR, androgen receptor; ARE, androgen response element; BrUTP, 5-bromo-uridine-5'-triphosphate; DBD, DNA binding domain; FRET, fluorescence resonance energy transfer; LBD, ligand binding domain; NTD, N-terminal transactivation domain; SR, steroid receptor.


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