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Small-molecule inhibition of Wnt signaling through activation of casein kinase 1α
Journal article   Peer reviewed

Small-molecule inhibition of Wnt signaling through activation of casein kinase 1α

Curtis A. Thorne, Alison J. Hanson, Judsen Schneider, Emilios Tahinci, Darren Orton, Christopher S. Cselenyi, Kristin K. Jernigan, Kelly C. Meyers, Brian I. Hang, Alex G. Waterson, …
Nature chemical biology, Vol.6(11), pp.829-836
11/01/2010
DOI: 10.1038/NCHEMBIO.453
PMCID: PMC3681608
PMID: 20890287
url
https://www.ncbi.nlm.nih.gov/pmc/articles/3681608View
Open Access

Abstract

Wnt/beta-catenin signaling is critically involved in metazoan development, stem cell maintenance and human disease. Using Xenopus laevis egg extract to screen for compounds that both stabilize Axin and promote beta-catenin turnover, we identified an FDA-approved drug, pyrvinium, as a potent inhibitor of Wnt signaling (EC(50) of similar to 10 nM). We show pyrvinium binds all casein kinase 1 (CK1) family members in vitro at low nanomolar concentrations and pyrvinium selectively potentiates casein kinase 1 alpha (CK1 alpha) kinase activity. CK1 alpha knockdown abrogates the effects of pyrvinium on the Wnt pathway. In addition to its effects on Axin and beta-catenin levels, pyrvinium promotes degradation of Pygopus, a Wnt transcriptional component. Pyrvinium treatment of colon cancer cells with mutation of the gene for adenomatous polyposis coli (APC) or beta-catenin inhibits both Wnt signaling and proliferation. Our findings reveal allosteric activation of CK1 alpha as an effective mechanism to inhibit Wnt signaling and highlight a new strategy for targeted therapeutics directed against the Wnt pathway.
Biochemistry & Molecular Biology Life Sciences & Biomedicine Science & Technology

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