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

• Jürgen Behrens

  J. Behrens, B.-A. Jerchow, M. Würtele, J. Grimm, C. Asbrand, R. Wirtz, W. Birchmeier, Max Delbrück Center for Molecular Medicine, Robert-Rössle-Strasse 10, 13122 Berlin, Germany.

• Boris-Alexander Jerchow

  J. Behrens, B.-A. Jerchow, M. Würtele, J. Grimm, C. Asbrand, R. Wirtz, W. Birchmeier, Max Delbrück Center for Molecular Medicine, Robert-Rössle-Strasse 10, 13122 Berlin, Germany.

• Martin Würtele

  J. Behrens, B.-A. Jerchow, M. Würtele, J. Grimm, C. Asbrand, R. Wirtz, W. Birchmeier, Max Delbrück Center for Molecular Medicine, Robert-Rössle-Strasse 10, 13122 Berlin, Germany.

• Jan Grimm

  J. Behrens, B.-A. Jerchow, M. Würtele, J. Grimm, C. Asbrand, R. Wirtz, W. Birchmeier, Max Delbrück Center for Molecular Medicine, Robert-Rössle-Strasse 10, 13122 Berlin, Germany.

• Christian Asbrand

  J. Behrens, B.-A. Jerchow, M. Würtele, J. Grimm, C. Asbrand, R. Wirtz, W. Birchmeier, Max Delbrück Center for Molecular Medicine, Robert-Rössle-Strasse 10, 13122 Berlin, Germany.

• Ralph Wirtz

  J. Behrens, B.-A. Jerchow, M. Würtele, J. Grimm, C. Asbrand, R. Wirtz, W. Birchmeier, Max Delbrück Center for Molecular Medicine, Robert-Rössle-Strasse 10, 13122 Berlin, Germany.

• Michael Kühl

  J. Behrens, B.-A. Jerchow, M. Würtele, J. Grimm, C. Asbrand, R. Wirtz, W. Birchmeier, Max Delbrück Center for Molecular Medicine, Robert-Rössle-Strasse 10, 13122 Berlin, Germany.

• Doris Wedlich

  J. Behrens, B.-A. Jerchow, M. Würtele, J. Grimm, C. Asbrand, R. Wirtz, W. Birchmeier, Max Delbrück Center for Molecular Medicine, Robert-Rössle-Strasse 10, 13122 Berlin, Germany.

• Walter Birchmeier

  J. Behrens, B.-A. Jerchow, M. Würtele, J. Grimm, C. Asbrand, R. Wirtz, W. Birchmeier, Max Delbrück Center for Molecular Medicine, Robert-Rössle-Strasse 10, 13122 Berlin, Germany.

抄録

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. In Xenopus embryos, conductin interfered with wnt-induced axis formation.

収録刊行物

• Science

  Science 280 (5363), 596-599, 1998-04-24

  American Association for the Advancement of Science (AAAS)

キーワード

• Multidisciplinary

詳細情報

• CRID: 1360574094130339968
• NII論文ID: 80010296309
• DOI: 10.1126/science.280.5363.596
• ISSN: 10959203
• ISSN: 00368075
• Web Site: https://www.science.org/doi/pdf/10.1126/science.280.5363.596
• データソース種別:
  • Crossref
  • CiNii Articles