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Nucleic Acids Research 2006 34(9):2570-2578; doi:10.1093/nar/gkl319
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Published online 12 May 2006

© The Author 2006. Published by Oxford University Press. All rights reserved
The online version of this article has been published under an open access model. Users are entitled to use, reproduce, disseminate, or display the open access version of this article for non-commercial purposes provided that: the original authorship is properly and fully attributed; the Journal and Oxford University Press are attributed as the original place of publication with the correct citation details given; if an article is subsequently reproduced or disseminated not in its entirety but only in part or as a derivative work this must be clearly indicated. For commercial re-use, please contact journals.permissions@oxfordjournals.org


Article

GAS41 interacts with transcription factor AP-2ß and stimulates AP-2ß-mediated transactivation

Xiaofeng Ding1, Changzheng Fan1, Jianlin Zhou1, Yingli Zhong1, Rushi Liu1, Kaiqun Ren1, Xiang Hu1, Chang Luo1, Shunyong Xiao1, Yeqi Wang1, Du Feng1 and Jian Zhang1,2,*

1 Key Laboratory of Protein Chemistry and Developmental Biology of State Education Ministry of China, College of Life Science, Hunan Normal University Changsha, Hunan 410081, China 2 Model Organism Division, E-Institutes of Shanghai Universities, Shanghai Second Medical University Shanghai 200025, China

*To whom correspondence should be addressed. Tel/Fax: +86 731 8872792; Email: zhangjian{at}hunnu.edu.cn

Received April 12, 2006. Revised April 13, 2006. Accepted April 13, 2006.

Transcription factor AP-2 regulates transcription of a number of genes involving mammalian development, differentiation and carcinogenesis. Recent studies have shown that interaction partners can modulate the transcriptional activity of AP-2 over the downstream targets. In this study, we reported the identification of GAS41 as an interaction partner of AP-2ß. We documented the interaction both in vivo by co-immunoprecipitation as well as in vitro through glutathione S-transferase (GST) pull-down assays. We also showed that the two proteins are co-localized in the nuclei of mammalian cells. We further mapped the interaction domains between the two proteins to the C-termini of both AP-2ß and GAS41, respectively. Furthermore, we have identified three critical residues of GAS41 that are important for the interaction between the two proteins. In addition, by transient co-expression experiments using reporter containing three AP-2 consensus binding sites in the promoter region, we found that GAS41 stimulates the transcriptional activity of AP-2ß over the reporter. Finally, electrophoretic mobility shift assay (EMSA) suggested that GAS41 enhances the DNA-binding activity of AP-2ß. Our data provide evidence for a novel cellular function of GAS41 as a transcriptional co-activator for AP-2ß.


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