Acetylation of beta-catenin by CREB-binding protein (CBP)

作者：Wolf D; Rodova M; Miska EA; Calvet JP; Kouzarides T^*

来源：JOURNAL OF BIOLOGICAL CHEMISTRY, 2002, 277(28): 25562-25567.

DOI：10.1074/jbc.M201196200

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 beta-catenin protein in vivo. beta-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 beta-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 beta-catenin. We show that mutation of this site leads specifically to an increase in the ability of beta-catenin to activate the c-myc gene but not other beta-catenin-regulated genes. This suggests that acetylation of beta-catenin is involved in regulating Wnt signaling in a promoter-specific fashion.

• 出版日期2002-7-12