MCB
Home Help [Feedback] [For Subscribers] [Archive] [Search] [Contents]
This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrowReprints and Permissions
Right arrow Copyright Information
Right arrow Books from ASM Press
Right arrow MicrobeWorld
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Labalette, C.
Right arrow Articles by Wei, Y.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Labalette, C.
Right arrow Articles by Wei, Y.

 Previous Article  |  Next Article 

Molecular and Cellular Biology, December 2004, p. 10689-10702, Vol. 24, No. 24
0270-7306/04/$08.00+0     DOI: 10.1128/MCB.24.24.10689-10702.2004
Copyright © 2004, American Society for Microbiology. All Rights Reserved.

Interaction and Functional Cooperation between the LIM Protein FHL2, CBP/p300, and ß-Catenin

Charlotte Labalette, Claire-Angélique Renard, Christine Neuveut, Marie-Annick Buendia,* and Yu Wei*

Unité d'Oncogenèse et Virologie Moléculaire, INSERM U.579, Institut Pasteur, Paris, France

Received 23 December 2003/ Returned for modification 9 February 2004/ Accepted 13 September 2004

Transcriptional activation of gene expression by Wnt signaling is driven by the association of ß-catenin with TCF/LEF factors and the recruitment of transcriptional coactivators. It has been shown that the LIM protein FHL2 and the acetyltransferase CBP/p300 individually stimulate ß-catenin transactivating activity and that ß-catenin is acetylated by p300. Here, we report that FHL2 and CBP/p300 synergistically enhanced ß-catenin/TCF-mediated transcription from Wnt-responsive promoters and that the acetyltransferase activity of CBP/p300 was involved in the cooperation. CBP/p300 interacted directly with FHL2, predominantly through the CH3 domain but not the histone acetyltransferase domain, and different regions of CBP/p300 were involved in FHL2 and ß-catenin binding. We provided evidence for the formation of a ternary complex by FHL2, CBP/p300, and ß-catenin and for colocalization of the three proteins in the nucleus. In murine FHL2–/– embryo fibroblasts, the transactivation activity of ß-catenin/TCF was markedly reduced, and this defect could be restored by exogenous expression of FHL2. However, CBP/p300 were still able to coactivate the ß-catenin/TCF complex in FHL2–/– cells, suggesting that FHL2 is dispensable for the coactivator function of CBP/p300 on ß-catenin. Furthermore, we found that FHL2 significantly increased acetylation of ß-catenin by p300 in vivo. Finally, we showed that FHL2, CBP/p300, and ß-catenin could synergistically activate androgen receptor-mediated transcription, indicating that the synergistic coactivator function is not restricted to TCF/LEF.

* Corresponding author. Mailing address: Unité d'Oncogenèse et Virologie Moléculaire, Institut Pasteur, 28 rue du Dr. Roux, 75724 Paris Cedex 15, France. Phone: 33-145 68 88 51. Fax: 33-145 68 89 43. E-mail for Yu Wei: ywei{at}pasteur.fr. E-mail for Marie-Annick Buendia: mbuendia{at}pasteur.fr.

Molecular and Cellular Biology, December 2004, p. 10689-10702, Vol. 24, No. 24
0022-538X/04/$08.00+0     DOI: 10.1128/MCB.24.24.10689-10702.2004
Copyright © 2004, American Society for Microbiology. All Rights Reserved.



This article has been cited by other articles:



Home Help [Feedback] [For Subscribers] [Archive] [Search] [Contents]
J. Bacteriol. J. Virol. Eukaryot. Cell
Microbiol. Mol. Biol. Rev. Clin. Vaccine Immunol. All ASM Journals

Copyright © 2004 by the American Society for Microbiology. All rights reserved.