Get 20M+ Full-Text Papers For Less Than $1.50/day. Start a 7-Day Trial for You or Your Team.

Learn More →

Androgen receptor serine 81 mediates Pin1 interaction and activity

Androgen receptor serine 81 mediates Pin1 interaction and activity Hormone-dependent tumors are characterized by deregulated activity of specific steroid receptors, allowing aberrant expression of many genes involved in cancer initiation, progression and metastasis. In prostate cancer, the androgen receptor (AR) protein has pivotal functions, and over the years it has been the target of different drugs. AR is a nuclear receptor whose activity is regulated by a phosphorylation mechanism controlled by hormone and growth factors. Following phosphorylation, AR interacts with many cofactors that closely control its function. Among such cofactors, Pin1 is a peptidyl-prolyl isomerase that is involved in the control of protein phosphorylation and has a prognostic value in prostate cancer. In the present study, we demonstrate that ARSer81 is involved in the interaction with Pin1, and that this interaction is important for the transcriptional activity of AR. Since Pin1 expression positively correlates with tumor grade, our results suggest that Pin1 can participate in this process by modulating AR function. http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png Cell Cycle Taylor & Francis

Androgen receptor serine 81 mediates Pin1 interaction and activity

6 pages

Loading next page...
 
/lp/taylor-francis/androgen-receptor-serine-81-mediates-pin1-interaction-and-activity-LApNmkqQpG

References (52)

Publisher
Taylor & Francis
Copyright
Copyright © 2012 Landes Bioscience
ISSN
1551-4005
eISSN
1538-4101
DOI
10.4161/cc.21730
pmid
22894932
Publisher site
See Article on Publisher Site

Abstract

Hormone-dependent tumors are characterized by deregulated activity of specific steroid receptors, allowing aberrant expression of many genes involved in cancer initiation, progression and metastasis. In prostate cancer, the androgen receptor (AR) protein has pivotal functions, and over the years it has been the target of different drugs. AR is a nuclear receptor whose activity is regulated by a phosphorylation mechanism controlled by hormone and growth factors. Following phosphorylation, AR interacts with many cofactors that closely control its function. Among such cofactors, Pin1 is a peptidyl-prolyl isomerase that is involved in the control of protein phosphorylation and has a prognostic value in prostate cancer. In the present study, we demonstrate that ARSer81 is involved in the interaction with Pin1, and that this interaction is important for the transcriptional activity of AR. Since Pin1 expression positively correlates with tumor grade, our results suggest that Pin1 can participate in this process by modulating AR function.

Journal

Cell CycleTaylor & Francis

Published: Sep 15, 2012

Keywords: phosphorylation; prostate cancer; androgen receptor; ARSer81; Pin1

There are no references for this article.