Acetylation of β-Catenin by CREB-binding Protein (CBP)*

By Daniel Wolf, M. Rodova, E. Miska, J. Calvet, Tony Kouzarides. Journal of Biological Chemistry, 2002

174 citations recorded by the source corpus.

Acetylation controls the activity of numerous proteins involved in regulating gene transcription as well as many other cellular processes. In this report we show that the CREB-binding protein (CBP) acetyltransferase acetylates β-catenin protein in vivo. β-Catenin is a central component of the Wnt signaling pathway, which is of key importance in development as well as being heavily implicated in a variety of human cancers. We show that the CBP-mediated acetylation of β-catenin occurs at a single site, lysine 49. Importantly, this lysine is frequently found mutated in cancer and is in a region of importance to the regulation of β-catenin. We show that mutation of this site leads specifically to an increase in the ability of β-catenin to activate the c-myc gene but not other β-catenin-regulated genes. This suggests that acetylation of β-catenin is involved in regulating Wnt signaling in a promoter-specific fashion.

Subfields: Molecular Biology

View Paper: https://www.semanticscholar.org/paper/14ff9cef93d7968190fa307def2c64315cf26aa5

Citations in the corpus

• The many faces and functions of β‐catenin (2012, unknown): “…Sokol, 2011; Archbold et al , 2012). b -Catenin can also be acetylated by CBP at Lys49; point mutations that block acetylation result in ectopic transcriptional activation of the target gene c-myc , an effect that seems to be specific to this target, since others were unaffected (Wolf et al , 2002).”