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An intrinsically labile α-helix abutting the BCL9-binding site of β-catenin is required for its inhibition by carnosic acid.

Published version
Peer-reviewed

Type

Article

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Authors

Rutherford, Trevor J 
Gupta, Deepti 
Veprintsev, Dmitry B 
Saxty, Barbara 

Abstract

Wnt/β-catenin signalling controls development and tissue homeostasis. Moreover, activated β-catenin can be oncogenic and, notably, drives colorectal cancer. Inhibiting oncogenic β-catenin has proven a formidable challenge. Here we design a screen for small-molecule inhibitors of β-catenin's binding to its cofactor BCL9, and discover five related natural compounds, including carnosic acid from rosemary, which attenuates transcriptional β-catenin outputs in colorectal cancer cells. Evidence from NMR and analytical ultracentrifugation demonstrates that the carnosic acid response requires an intrinsically labile α-helix (H1) amino-terminally abutting the BCL9-binding site in β-catenin. Similarly, in colorectal cancer cells with hyperactive β-catenin signalling, carnosic acid targets predominantly the transcriptionally active ('oncogenic') form of β-catenin for proteasomal degradation in an H1-dependent manner. Hence, H1 is an 'Achilles' Heel' of β-catenin, which can be exploited for destabilization of oncogenic β-catenin by small molecules, providing proof-of-principle for a new strategy for developing direct inhibitors of oncogenic β-catenin.

Description

Keywords

Abietanes, Binding Sites, Cell Line, Tumor, Colorectal Neoplasms, Crystallography, X-Ray, HEK293 Cells, HeLa Cells, Humans, Neoplasm Proteins, Nuclear Magnetic Resonance, Biomolecular, Plant Extracts, Proteasome Endopeptidase Complex, Protein Stability, Rosmarinus, Signal Transduction, Transcription Factors, Wnt Proteins, beta Catenin

Journal Title

Nat Commun

Conference Name

Journal ISSN

2041-1723
2041-1723

Volume Title

3

Publisher

Springer Science and Business Media LLC