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Nucleic Acids Research Advance Access originally published online on December 18, 2008
Nucleic Acids Research 2009 37(3):832-848; doi:10.1093/nar/gkn941
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Nucleic Acids Research, 2009, Vol. 37, No. 3 832-848
© 2008 The Author(s)
This is an Open Access article distributed under the terms of the Creative Commons Attribution Non-Commercial License (http://creativecommons.org/licenses/by-nc/2.0/uk/) which permits unrestricted non-commercial use, distribution, and reproduction in any medium, provided the original work is properly cited.

Gene regulation, Chromatin and Epigenetics

A feedback regulatory loop between methyltransferase PRMT1 and orphan receptor TR3

Na-zi Lei, Xiao-yan Zhang, Hang-zi Chen, Yuan Wang, Yan-yan Zhan, Zhong-hui Zheng, Yue-mao Shen and Qiao Wu*

Key Laboratory of the Ministry of Education for Cell Biology and Tumor Cell Engineering, School of Life Sciences, Xiamen University, Xiamen 361005, Fujian Province, China

*To whom correspondence should be addressed. Tel: +86 592 2187959; Fax: +86 592 2086630; Email: qiaow{at}xmu.edu.cn

Received September 28, 2008. Revised November 5, 2008. Accepted November 6, 2008.

PRMT1, an arginine methyltransferase, plays an important role in numerous cellular processes. In this study, we demonstrate a feedback regulatory loop between PRMT1 and the orphan receptor TR3. Unlike another orphan receptor HNF4, TR3 is not methylated by PRMT1 although they physically interact with each other. By delaying the TR3 protein degradation, PRMT1 binding leads to the elevation of TR3 cellular protein level, thereby enhances the DNA binding and transactivation activity of TR3 in a non-methyltransferase manner. Another coactivator SRC-2 acts synergistically with PRMT1 to regulate TR3 functions. In turn, TR3 binding to the catalytic domain of PRMT1 causes an inhibition of the PRMT1 methyltransferase activity. This repression results in the functional changes in some of PRMT1 substrates, including STAT3 and Sam68. The negative regulation of PRMT1 by TR3 was further confirmed in both TR3-knockdown cells and TR3-knockout mice with the use of an agonist for TR3. Taken together, our study not only identifies a regulatory role of PRMT1, independent on methyltransferase activity, in TR3 transactivation, but also characterizes a novel function of TR3 in the repression of PRMT1 methyltransferase activity.

The authors wish it to be known that, in their opinion, the first two authors should be regarded as joint First Authors


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