Acetylation of human TCF4 (TCF7L2) proteins attenuates inhibition by the HBP1 repressor and induces a conformational change in the TCF4::DNA complex
15.04.2013
Elfert S, Weise A, Bruser K, Biniossek ML, Jägle S, Senghaas N, Hecht A.
PLoS One. 2013;8(4):e61867
In this study we investigated whether effector proteins of the Wnt/?-catenin signal transduction pathway can be posttranslationally modified by the lysine acetyltransferases p300 or CBP. By immunoblotting, mass spectrometry and mutational analyses we identified lysine K150 in the transcription factor TCF4 (also known as TCF7L2) as a target for CBP-mediated acetylation. K150 acetylation alters the structure of the TCF4::DNA complex and protects TCF4 against the inhibitory influence of the HBP1 tumor suppressor. Acetylation of TCF4 by CBP is a novel mechanism to regulate TCF4 transcriptional function.
