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Nucleic Acids Research 2005 33(16):5271-5290; doi:10.1093/nar/gki837
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Published online 16 September 2005

© The Author 2005. 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{at}oxfordjournals.org

Article

Binding of serum response factor to cystic fibrosis transmembrane conductance regulator CArG-like elements, as a new potential CFTR transcriptional regulation pathway

Céline René, Magali Taulan, Florence Iral, Julien Doudement, Aurore L'Honoré1,2, Catherine Gerbon, Jacques Demaille3, Mireille Claustres and Marie-Catherine Romey*

Laboratoire de Génétique Moléculaire et Chromosomique, Institut Universitaire de Recherche Clinique Montpellier, France 1Laboratoire de Prolifération et Différentiation Cellulaire, Institut de Génétique Humaine Montpellier, France 2Laboratoire de Génétique Moléculaire, Institut de Recherches Cliniques de Montréal Quebec, Canada 3Centre de Séquençage Génomique, Institut de Génétique Humaine Montpellier, France

*To whom correspondence should be addressed. Tel: +33 4 67 41 53 60; Fax: +33 4 67 41 53 65; Email: Marie-Catherine.Romey{at}igh.cnrs.fr

Revised August 25, 2005. Accepted August 30, 2005.

CFTR expression is tightly controlled by a complex network of ubiquitous and tissue-specific cis-elements and trans-factors. To better understand mechanisms that regulate transcription of CFTR, we examined transcription factors that specifically bind a CFTR CArG-like motif we have previously shown to modulate CFTR expression. Gel mobility shift assays and chromatin immunoprecipitation analyses demonstrated the CFTR CArG-like motif binds serum response factor both in vitro and in vivo. Transient co-transfections with various SRF expression vector, including dominant-negative forms and small interfering RNA, demonstrated that SRF significantly increases CFTR transcriptional activity in bronchial epithelial cells. Mutagenesis studies suggested that in addition to SRF other co-factors, such as Yin Yang 1 (YY1) previously shown to bind the CFTR promoter, are potentially involved in the CFTR regulation. Here, we show that functional interplay between SRF and YY1 might provide interesting perspectives to further characterize the underlying molecular mechanism of the basal CFTR transcriptional activity. Furthermore, the identification of multiple CArG binding sites in highly conserved CFTR untranslated regions, which form specific SRF complexes, provides direct evidence for a considerable role of SRF in the CFTR transcriptional regulation into specialized epithelial lung cells.

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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