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J Biol Chem. 2002 May 17;277(20):17933-43. Epub 2002 Feb 20.

The androgen receptor can promote beta-catenin nuclear translocation independently of adenomatous polyposis coli.

Author information

1
Prostate Research Centre, 2660 Oak St., Jack Bell Research, Vancouver General Hospital, Vancouver, British Columbia V6H 3Z6, Canada. djm@interchange.ubc.ca

Abstract

We provide evidence that the androgen receptor (AR) can promote nuclear translocation of beta-catenin in LNCaP and PC3 prostate cancer cells. Using AR-expressing cells (LNCaP) and non-AR-expressing cells (PC3) we showed by time course cell fractionation that the AR can shuttle beta-catenin into the nucleus when exposed to exogenous androgen. Cells exposed to the synthetic androgen, R1881, show distinct, punctate, nuclear co-localization of the AR and beta-catenin. We further showed that the AR does not interact with adenomatous polyposis coli or glycogen synthase kinase-3beta and, therefore, conclude that androgen-mediated transport of beta-catenin occurs through a distinct pathway. The minimal necessary components of the AR and beta-catenin required for binding nuclear accumulation of beta-catenin nuclear import appears to be the DNA/ligand binding regions and the Armadillo repeats of beta-catenin. We also employed a novel DNA binding assay to illustrate that beta-catenin has the capacity to bind to the probasin promoter in an AR-dependent manner. The physiological relevance of AR-mediated transport of beta-catenin and binding to an AR promoter appeared to be a substantial increase in AR transcriptional reporter activity. AR-mediated import represents a novel mode of nuclear accumulation of beta-catenin.

PMID:
11856748
DOI:
10.1074/jbc.M200135200
[Indexed for MEDLINE]
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