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Nucleic Acids Research Advance Access originally published online on November 11, 2006
Nucleic Acids Research 2006 34(21):6314-6326; doi:10.1093/nar/gkl914
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Nucleic Acids Research, 2006, Vol. 34, No. 21 6314-6326
© 2006 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.

Molecular Biology

Potentiation of Smad-mediated transcriptional activation by the RNA-binding protein RBPMS

Yan Sun, Lihua Ding, Hao Zhang, Juqiang Han, Xiao Yang, Jinghua Yan, Yunfeng Zhu1, Jiezhi Li, Haifeng Song2 and Qinong Ye*

Beijing Institute of Biotechnology, Beijing 100850 People's Republic of China 1 The 307th Hospital, Beijing 100071 People's Republic of China 2 Beijing Institute of Radiation Medicine, Beijing 100850 People's Republic of China

*To whom correspondence should be addressed. Tel: +8610 6818 0809; Fax: +8610 6824 8045; Email: yeqn{at}nic.bmi.ac.cn

Received September 25, 2006. Revised October 15, 2006. Accepted October 16, 2006.

Smad2, Smad3 and Smad4 proteins are considered to be key mediators of transforming growth factor-ß (TGF-ß) signaling. However, the identities of the Smad partners mediating TGF-ß signaling are not fully understood. Here, we show that RNA-binding protein with multiple splicing (RBPMS), a member of the RNA-binding protein family, physically interacts with Smad2, Smad3 and Smad4 both in vitro and in vivo. The presence of TGF-ß increases the binding of RBPMS with these Smad proteins. Consistent with the binding results, overexpression of RBPMS enhances Smad-dependent transcriptional activity in a TGF-ß-dependent manner, whereas knockdown of RBPMS decreases this activity. RBPMS interacts with TGF-ß receptor type I (TßR-I), increases phosphorylation of C-terminal SSXS regions in Smad2 and Smad3, and promotes the nuclear accumulation of the Smad proteins. Moreover, RBPMS fails to enhance the transcriptional activity of Smad2 and Smad3 that lack the C-terminal phosphorylation sites. Our data provide the first evidence for an RNA-binding protein playing a role in regulation of Smad-mediated transcriptional activity and suggest that RBPMS stimulates Smad-mediated transactivation possibly through enhanced phosphorylation of Smad2 and Smad3 at the C-terminus and promotion of the nuclear accumulation of the Smad proteins.

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


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