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J. Biol. Chem. 277 (13): 11336-11344

© 2002 by The American Society for Biochemistry and Molecular Biology, Inc.

Linking beta -Catenin to Androgen-signaling Pathway*

Fajun YangDagger , Xiaoyu Li§, Manju SharmaDagger , Carl Y. Sasaki, Dan L. Longo, Bing Lim§, and Zijie SunDagger ||

From the Dagger  Department of Surgery and Department of Genetics, Stanford University School of Medicine, Stanford, California 94305-5328, the § Division of Hematology/Oncology, Department of Medicine, Beth Israel Deaconess Medical Center, Boston, Massachusetts 02115, and the  Laboratory of Immunology, NIA, National Institutes of Health, Baltimore, Maryland 21224

The androgen-signaling pathway is important for the growth and progression of prostate cancer cells. The growth-promoting effects of androgen on prostate cells are mediated mostly through the androgen receptor (AR). There is increasing evidence that transcription activation by AR is mediated through interaction with other cofactors. beta -Catenin plays a critical role in embryonic development and tumorigenesis through its effects on E-cadherin-mediated cell adhesion and Wnt-dependent signal transduction. Here, we demonstrate that a specific protein-protein interaction occurs between beta -catenin and AR. Unlike the steroid hormone receptor coactivator 1 (SRC1), beta -catenin showed a strong interaction with AR but not with other steroid hormone receptors such as estrogen receptor alpha , progesterone receptor beta , and glucocorticoid receptor. The ligand binding domain of AR and the NH2 terminus combined with the first six armadillo repeats of beta -catenin were shown to be necessary for the interaction. Through this specific interaction, beta -catenin augments the ligand-dependent activity of AR in prostate cancer cells. Moreover, expression of E-cadherin in E-cadherin-negative prostate cancer cells results in redistribution of the cytoplasmic beta -catenin to the cell membrane and reduction of AR-mediated transcription. These data suggest that loss of E-cadherin can elevate the cellular levels of beta -catenin in prostate cancer cells, which may directly contribute to invasiveness and a more malignant tumor phenotype by augmenting AR activity during prostate cancer progression.

* This work was supported by National Institutes of Health Grants CA70297 (to Z. S.) and DK47636 and DK54417 (to B. L.) and by Department of Army Prostate Cancer Grant PC01-0690.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.

|| To whom correspondence should be addressed: Depts. of Surgery and Genetics, R135, Edwards Bldg., Stanford University School of Medicine, Stanford, CA 94305-5328. E-mail: zsun@stanford.edu.

Copyright © 2002 by The American Society for Biochemistry and Molecular Biology, Inc.

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Mol. Endocrinol. 17, 507-519
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{beta}-Catenin Binds to the Activation Function 2 Region of the Androgen Receptor and Modulates the Effects of the N-Terminal Domain and TIF2 on Ligand-Dependent Transcription.
L.-N. Song, R. Herrell, S. Byers, S. Shah, E. M. Wilson, and E. P. Gelmann (2003)
Mol. Cell. Biol. 23, 1674-1687
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Identification of the LIM Protein FHL2 as a Coactivator of beta -Catenin.
Y. Wei, C.-A. Renard, C. Labalette, Y. Wu, L. Levy, C. Neuveut, X. Prieur, M. Flajolet, S. Prigent, and M.-A. Buendia (2003)
J. Biol. Chem. 278, 5188-5194
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Phosphatidylinositol 3-Kinase/Akt Stimulates Androgen Pathway through GSK3beta Inhibition and Nuclear beta -Catenin Accumulation.
M. Sharma, W. W. Chuang, and Z. Sun (2002)
J. Biol. Chem. 277, 30935-30941
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Liganded Androgen Receptor Interaction with beta -Catenin. NUCLEAR CO-LOCALIZATION AND MODULATION OF TRANSCRIPTIONAL ACTIVITY IN NEURONAL CELLS.
J. E. Pawlowski, J. R. Ertel, M. P. Allen, M. Xu, C. Butler, E. M. Wilson, and M. E. Wierman (2002)
J. Biol. Chem. 277, 20702-20710
   Abstract »    Full Text »    PDF »

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