Acetylation of human TCF4 (TCF7L2) proteins attenuates inhibition by the HBP1 repressor and induces a conformational change in the TCF4::DNA complex (eBook, 2013) [WorldCat.org]
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Acetylation of human TCF4 (TCF7L2) proteins attenuates inhibition by the HBP1 repressor and induces a conformational change in the TCF4::DNA complex

Author: Susanne Claudia ElfertAndreas WeiseKatja RoseMartin Lothar BiniossekSabine JägleAll authors
Publisher: Freiburg Universität 2013
Edition/Format:   eBook : Document : EnglishView all editions and formats
Summary:
Abstract: The members of the TCF/LEF family of DNA-binding proteins are components of diverse gene regulatory networks. As<br>nuclear effectors of Wnt/ß-catenin signaling they act as assembly platforms for multimeric transcription complexes that either repress or activate gene expression. Previously, it was shown that several aspects of TCF/LEF protein function are regulated by post-translational modification.  Read more...
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Material Type: Document, Internet resource
Document Type: Internet Resource, Computer File
All Authors / Contributors: Susanne Claudia Elfert; Andreas Weise; Katja Rose; Martin Lothar Biniossek; Sabine Jägle; Niklas Julius Senghaas; Andreas Hecht; Spemann Graduate School of Biology and Medicine; Albert-Ludwigs-Universität Freiburg Institut für Molekulare Medizin und Zellforschung; Albert-Ludwigs-Universität Freiburg Institut für Biologie II; Albert-Ludwigs-Universität Freiburg Centre for Biological Signalling Studies; Albert-Ludwigs-Universität Freiburg Fakultät für Biologie; Albert-Ludwigs-Universität Freiburg
OCLC Number: 1003225611
Notes: PLoS ONE. 8, 4 (2013), e61867, DOI 10.1371/journal.pone.0061867, issn: 1932-6203
IN COPYRIGHT http://rightsstatements.org/page/InC/1.0 rs
Description: Online-Ressource

Abstract:

Abstract: The members of the TCF/LEF family of DNA-binding proteins are components of diverse gene regulatory networks. As<br>nuclear effectors of Wnt/ß-catenin signaling they act as assembly platforms for multimeric transcription complexes that either repress or activate gene expression. Previously, it was shown that several aspects of TCF/LEF protein function are regulated by post-translational modification. The association of TCF/LEF family members with acetyltransferases and deacetylases prompted us to investigate whether vertebrate TCF/LEF proteins are subject to acetylation. Through co-expression with p300 and CBP and subsequent analyses using mass spectrometry and immunodetection with anti-acetyl-lysine antibodies we show that TCF4 can be acetylated at lysine K150 by CBP. K150<br>acetylation is restricted to TCF4E splice variants and requires the simultaneous presence of ß-catenin and the unique TCF4E C-terminus. To examine the functional consequences of K150 acetylation we substituted K150 with amino acids representing the non-acetylated and acetylated states. Reporter gene assays based on Wnt/ß-catenin-responsive promoter regions did not indicate a general role of K150<br>acetylation in transactivation by TCF4E. However, in the presence of CBP, non-acetylatable TCF4E with a K150<br>R substitution was more susceptible to inhibition by the HBP-1 repressor protein compared to wild-type TCF4E. Acetylation of K150 using a bacterial expression system or amino acid substitutions at K150 alter the electrophoretic properties of TCF4E::DNA complexes. This result suggests that K150<br>acetylation leads to a conformational change that may also represent the mechanism whereby acetylated TCF4E acquires resistance against HBP1. In summary, TCF4 not only recruits acetyltransferases but is also a substrate for these enzymes. The fact that acetylation affects only a subset of TCF4 splice variants and is mediated preferentially by CBP suggests that the conditional acetylation of TCF4E is a novel regulatory mechanism that diversifies the transcriptional output of Wnt/ß-catenin signaling in response to changing intracellular signaling milieus

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