Functional Interaction of an Axin Homolog, Conductin, with β-Catenin, APC, and GSK3β

作者：Jürgen Behrens, Boris Jerchow, Martin Würtele, Jan Grimm, Christian Asbrand, Ralph M. Wirtz, Michael Kühl, Doris Wedlich, Walter Birchmeier · 发表于：Science · 年份：1998 · DOI：10.1126/science.280.5363.596 · 被引用次数：1275 · 研究领域：Wnt/β-catenin signaling in development and cancer、Cancer-related gene regulation、RNA Research and Splicing

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.