Previous Article | Next Article ![]()
Molecular and Cellular Biology, December 1999, p. 8383-8392, Vol. 19, No. 12
Molecular Endocrinology Laboratory, Imperial
Cancer Research Fund, London WC2A 3PX, United
Kingdom,1 and Afdeling Biochemie, Campus
Gasthuisberg, 300 Leuven, Belgium2
Received 20 May 1999/Returned for modification 23 June
1999/Accepted 14 September 1999
The androgen receptor is unusual among nuclear receptors in that
most, if not all, of its activity is mediated via the constitutive activation function in the N terminus. Here we demonstrate that p160
coactivators such as SRC1 (steroid receptor coactivator 1) interact
directly with the N terminus in a ligand-independent manner via a
conserved glutamine-rich region between residues 1053 and 1123. Although SRC1 is capable of interacting with the ligand-binding domain
by means of LXXLL motifs, this interaction is not essential since an
SRC1 mutant with no functional LXXLL motifs retains its ability to
potentiate androgen receptor activity. In contrast, mutants lacking the
glutamine-rich region are inactive, indicating that this region is both
necessary and sufficient for recruitment of SRC1 to the androgen
receptor. This recruitment is in direct contrast to the recruitment of
SRC1 to the estrogen receptor, which requires interaction with the
ligand-binding domain.
0270-7306/99/$04.00+0
Copyright © 1999, American Society for Microbiology. All rights reserved.
The AF1 and AF2 Domains of the Androgen Receptor
Interact with Distinct Regions of SRC1

and
*
Corresponding author. Mailing address: Molecular
Endocrinology Laboratory, Imperial Cancer Research Fund, 44 Lincoln's
Inn Fields, London WC2A 3PX, United Kingdom. Phone: 44 171 269 3280. Fax: 44 171 269 3094. E-mail: m.parker{at}icrf.icnet.uk.
Present address: Prostate Cancer Research Group, Department of
Cancer Medicine, Imperial College School of Medicine, Hammersmith Hospital, London W12 0NN, United Kingdom.
Present address: Department of Biochemistry, University of
Leicester, Leicester LE1 7RH, United Kingdom.
This article has been cited by other articles:
| J. Bacteriol. | J. Virol. | Eukaryot. Cell |
|---|
| Microbiol. Mol. Biol. Rev. | Clin. Vaccine Immunol. | All ASM Journals |
|---|