Functional Interaction of an Axin Homolog, Conductin, with β-Catenin, APC, and GSK3β
Jürgen Behrens(Universität Ulm), Boris Jerchow(Universität Ulm), Martin Würtele(Universität Ulm), Jan Grimm(Universität Ulm), Christian Asbrand(Universität Ulm), Ralph M. Wirtz(Universität Ulm), Michael Kühl(Universität Ulm), Doris Wedlich(Universität Ulm), Walter Birchmeier(Universität Ulm)
Cited by 1,269
Abstract
Control of stability of beta-catenin is central in the wnt signaling pathway. Here, the protein conductin was found to form a complex with both beta-catenin and the tumor suppressor gene product adenomatous polyposis coli (APC). Conductin induced beta-catenin degradation, whereas mutants of conductin that were deficient in complex formation stabilized beta-catenin. Fragments of APC that contained a conductin-binding domain also blocked beta-catenin degradation. Thus, conductin is a component of the multiprotein complex that directs beta-catenin to degradation and is located downstream of APC. In Xenopus embryos, conductin interfered with wnt-induced axis formation.