JME
HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
QUICK SEARCH:   [advanced]


     

Journal of Molecular Endocrinology (2008) 40, 199-210    DOI: 10.1677/JME-07-0132
© 2008 Society for Endocrinology
This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Citing Articles
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Tan, B.
Right arrow Articles by Bigsby, R. M
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Tan, B.
Right arrow Articles by Bigsby, R. M

Striatin-3{gamma} inhibits estrogen receptor activity by recruiting a protein phosphatase

 Bailin Tan, Xinghua Long1, Harikrishna Nakshatri2, Kenneth P Nephew1 and Robert M Bigsby

Department of Obstetrics and Gynecology University School of Medicine, 975 West Walnut Street (IB360), Indianapolis, Indiana 46202, USA1 Department of Medical Sciences Program, Indiana University School of Medicine, Bloomington, Indianapolis, Indiana 47405, USA2 Department of Surgery, Indiana University School of Medicine, Indianapolis, Indiana 46202, USA

(Correspondence should be addressed to R M Bigsby; Email: rbigsby{at}iupui.edu)

A splicing variant of rat striatin-3 (rSTRN3{gamma}) was found to associate with estrogen receptor-{alpha} (ER{alpha}) in a ligand-dependent manner. In two-hybrid and pull-down analyses, estradiol induced an interaction between rSTRN3{gamma} and ER{alpha}. STRN3{gamma} protein was found in nuclear extracts from rat uterus and human cell lines. Overexpression of rSTRN3{gamma} induced a decrease in ER{alpha} transcriptional activity but had no effect on ERβ activity. Immunoprecipitation analyses showed that rSTRN3{gamma} interacts with both the ER{alpha} and the catalytic subunit of protein phosphatase 2A (PP2A(C)). The transrepressor action of rSTRN3{gamma} was overcome by okadaic acid, an inhibitor of PP2A(C), and by cotransfection of PP2A(C) siRNA. rSTRN3{gamma} caused dephosphorylation of ER{alpha} at serine 118 and this was abrogated by okadaic acid. ER{alpha} lacking phosphorylation sites at either serine 118 or 167 was insensitive to the corepressor action of rSTRN3{gamma}. These observations suggest that an rSTRN3{gamma}-PP2A(C) complex is recruited to agonist-activated ER{alpha}, thereby leading to its dephosphorylation and inhibiting transcription.






HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
Copyright © 2008 by the Society for Endocrinology.