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

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.

Pubmed ID: 9554852

Authors

  • Behrens J
  • Jerchow BA
  • Würtele M
  • Grimm J
  • Asbrand C
  • Wirtz R
  • Kühl M
  • Wedlich D
  • Birchmeier W

Journal

Science (New York, N.Y.)

Publication Data

April 24, 1998

Associated Grants

None

Mesh Terms

  • Adenomatous Polyposis Coli Protein
  • Amino Acid Sequence
  • Animals
  • Axin Protein
  • Binding Sites
  • Body Patterning
  • Calcium-Calmodulin-Dependent Protein Kinases
  • Cytoskeletal Proteins
  • Glycogen Synthase Kinase 3
  • Humans
  • Mice
  • Molecular Sequence Data
  • Mutation
  • Phosphorylation
  • Proteins
  • Proto-Oncogene Proteins
  • Repressor Proteins
  • Signal Transduction
  • Trans-Activators
  • Tumor Cells, Cultured
  • Xenopus
  • Xenopus Proteins
  • beta Catenin