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GAS41 interacts with transcription factor AP-2β and stimulates AP-2β-mediated transactivation
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 th...
Autores principales: | , , , , , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Oxford University Press
2006
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3303177/ https://www.ncbi.nlm.nih.gov/pubmed/16698963 http://dx.doi.org/10.1093/nar/gkl319 |
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author | Ding, Xiaofeng Fan, Changzheng Zhou, Jianlin Zhong, Yingli Liu, Rushi Ren, Kaiqun Hu, Xiang Luo, Chang Xiao, Shunyong Wang, Yeqi Feng, Du Zhang, Jian |
author_facet | Ding, Xiaofeng Fan, Changzheng Zhou, Jianlin Zhong, Yingli Liu, Rushi Ren, Kaiqun Hu, Xiang Luo, Chang Xiao, Shunyong Wang, Yeqi Feng, Du Zhang, Jian |
author_sort | Ding, Xiaofeng |
collection | PubMed |
description | 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-2β. 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-2β 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-2β over the reporter. Finally, electrophoretic mobility shift assay (EMSA) suggested that GAS41 enhances the DNA-binding activity of AP-2β. Our data provide evidence for a novel cellular function of GAS41 as a transcriptional co-activator for AP-2β. |
format | Online Article Text |
id | pubmed-3303177 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2006 |
publisher | Oxford University Press |
record_format | MEDLINE/PubMed |
spelling | pubmed-33031772012-03-14 GAS41 interacts with transcription factor AP-2β and stimulates AP-2β-mediated transactivation Ding, Xiaofeng Fan, Changzheng Zhou, Jianlin Zhong, Yingli Liu, Rushi Ren, Kaiqun Hu, Xiang Luo, Chang Xiao, Shunyong Wang, Yeqi Feng, Du Zhang, Jian Nucleic Acids Res Article 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-2β. 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-2β 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-2β over the reporter. Finally, electrophoretic mobility shift assay (EMSA) suggested that GAS41 enhances the DNA-binding activity of AP-2β. Our data provide evidence for a novel cellular function of GAS41 as a transcriptional co-activator for AP-2β. Oxford University Press 2006 /pmc/articles/PMC3303177/ /pubmed/16698963 http://dx.doi.org/10.1093/nar/gkl319 Text en © 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 |
spellingShingle | Article Ding, Xiaofeng Fan, Changzheng Zhou, Jianlin Zhong, Yingli Liu, Rushi Ren, Kaiqun Hu, Xiang Luo, Chang Xiao, Shunyong Wang, Yeqi Feng, Du Zhang, Jian GAS41 interacts with transcription factor AP-2β and stimulates AP-2β-mediated transactivation |
title | GAS41 interacts with transcription factor AP-2β and stimulates AP-2β-mediated transactivation |
title_full | GAS41 interacts with transcription factor AP-2β and stimulates AP-2β-mediated transactivation |
title_fullStr | GAS41 interacts with transcription factor AP-2β and stimulates AP-2β-mediated transactivation |
title_full_unstemmed | GAS41 interacts with transcription factor AP-2β and stimulates AP-2β-mediated transactivation |
title_short | GAS41 interacts with transcription factor AP-2β and stimulates AP-2β-mediated transactivation |
title_sort | gas41 interacts with transcription factor ap-2β and stimulates ap-2β-mediated transactivation |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3303177/ https://www.ncbi.nlm.nih.gov/pubmed/16698963 http://dx.doi.org/10.1093/nar/gkl319 |
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