Functional interaction of an axin homolog, conductin, with β-catenin, APC, and GSK3β

J Behrens, BA Jerchow, M Würtele, J Grimm… - Science, 1998 - science.org
J Behrens, BA Jerchow, M Würtele, J Grimm, C Asbrand, R Wirtz, M Kühl, D Wedlich…
Science, 1998science.org
Control of stability of β-catenin is central in the wnt signaling pathway. Here, the protein
conductin was found to form a complex with both β-catenin and the tumor suppressor gene
product adenomatous polyposis coli (APC). Conductin induced β-catenin degradation,
whereas mutants of conductin that were deficient in complex formation stabilized β-catenin.
Fragments of APC that contained a conductin-binding domain also blocked β-catenin
degradation. Thus, conductin is a component of the multiprotein complex that directs β …
Control of stability of β-catenin is central in the wnt signaling pathway. Here, the protein conductin was found to form a complex with both β-catenin and the tumor suppressor gene product adenomatous polyposis coli (APC). Conductin induced β-catenin degradation, whereas mutants of conductin that were deficient in complex formation stabilized β-catenin. Fragments of APC that contained a conductin-binding domain also blocked β-catenin degradation. Thus, conductin is a component of the multiprotein complex that directs β-catenin to degradation and is located downstream of APC. InXenopus embryos, conductin interfered with wnt-induced axis formation.
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