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Functional interaction of an axin homolog, conductin, with beta-catenin, APC, and GSK3beta

Item Type:Article
Title:Functional interaction of an axin homolog, conductin, with beta-catenin, APC, and GSK3beta
Creators Name:Behrens, J. and Jerchow, B.A. and Wuertele, M. and Grimm, J. and Asbrand, C. and Wirtz, R. and Kuehl, M. and Wedlich, D. and Birchmeier, W.
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.
Keywords:Adenomatous Polyposis Coli Protein, Amino Acid Sequence, Axin Protein, beta Catenin, Binding Sites, Body Patterning, Calcium-Calmodulin-Dependent Protein Kinases, Cultured Tumor Cells, Cytoskeletal Proteins, Glycogen Synthase Kinase 3, Molecular Sequence Data, Mutation, Phosphorylation, Proteins, Proto-Oncogene Proteins, Repressor Proteins, Signal Transduction, Trans-Activators, Xenopus, Xenopus Proteins, Animals, Mice
Source:Science
ISSN:0036-8075
Publisher:American Association for the Advancement of Science (U.S.A.)
Volume:280
Number:5363
Page Range:596-599
Date:24 April 1998
Official Publication:https://doi.org/10.1126/science.280.5363.596
PubMed:View item in PubMed

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