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    Science. 1996 May 17;272(5264):1023-6.

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

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

    Onyx Pharmaceuticals, Richmond, CA 94806, USA.

    Comment in:

    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.

    PMID: 8638126 [PubMed - indexed for MEDLINE]

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