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. 1996 May 17;272(5264):1023-6.
doi: 10.1126/science.272.5264.1023.

Binding of GSK3beta to the APC-beta-catenin complex and regulation of complex assembly

B Rubinfeld  1 , I Albert, E Porfiri, C Fiol, S Munemitsu, P Polakis
Affiliations

Binding of GSK3beta to the APC-beta-catenin complex and regulation of complex assembly

B Rubinfeld et al. Science. .

Abstract

The adenomatous polyposis coli gene (APC) is mutated in most colon cancers. The APC protein binds to the cellular adhesion molecule beta-catenin, which is a mammalian homolog of ARMADILLO, a component of the WINGLESS signaling pathway in Drosophila development. Here it is shown that when beta-catenin is present in excess, APC binds to another component of the WINGLESS pathway, glycogen synthase kinase 3beta (GSK3beta), a mammalian homolog of Drosophila ZESTE WHITE 3. APC was a good substrate for GSK3 beta in vitro, and the phosphorylation sites were mapped to the central region of APC. Binding of beta-catenin to this region was dependent on phosphorylation by GSK3 beta.

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