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Wnts are secreted lipid-modified glycoproteins that regulate cell proliferation, cell polarity, and cell fate determination through a range of pathways. The most characterized pathway is the Wnt/β-catenin pathway, which functions by regulating the phosphorylation and degradation of intracellular β-catenin. The Wnt/β-catenin pathway is triggered by Wnts (Wnt1, Wnt3a and Wnt8) interacting with Frizzled (Fz) receptors and low density lipoprotein receptorrelated protein5/6 (LRP5/6) co-receptor, which then promotes the recruitment of Dishevelled (Dvl) to Fz. This leads to LRP5/6 phosphorylation, which induces an interaction of the Axin complex with phosphorylated LRP5/6, resulting in inhibition of the Axin complex-mediated βcatenin phosphorylation/degradation. Accumulated β-catenin is translocated into the nucleus, where it forms a complex with the T cell factor/lymphocyte enhancer factor family of transcription factors to activate its target genes, such as cmyc, cyclin D1, and metalloproteinase-7. In the absence of Wnt, casein kinase 1 (CK1) and glycogen synthase kinase-3β (GSK-3β) phosphorylate sequentially the aminoterminal region of β-catenin in a complex with the scaffolding protein Axin and the tumor suppressor protein adenomatous polyposis coli (APC). Phosphorylated βcatenin is recognized by the F-box β-transducin repeat-

Identification of Antimycin A as a Small Molecule Inhibitor of the Wnt/β-catenin Pathway