Open AccessProteomic analysis identifies that 14-3-3ζ interacts with β-catenin and facilitates its activation by Akt
Author(s) -
Qiang Tian,
Megan C. Feetham,
Wanyu Tao,
Xi He,
Linheng Li,
Ruedi Aebersold,
Leroy Hood
Publication year - 2004
Publication title -
proceedings of the national academy of sciences of the united states of america
Language(s) - English
Resource type - Journals
eISSN - 1091-6490
pISSN - 0027-8424
DOI - 10.1073/pnas.0406499101
Subject(s) - wnt signaling pathway , protein kinase b , catenin , microbiology and biotechnology , effector , stem cell , biology , beta catenin , phosphorylation , transcription factor , embryonic stem cell , cytoplasm , signal transduction , cancer research , biochemistry , gene
beta-Catenin is a central effector of Wnt signaling in embryonic and stem cell development and in tumorigenesis. Here, through a mass spectrometric analysis of a beta-catenin protein complex, we identified 12 proteins as putative beta-catenin interactors. We show that one of them, 14-3-3zeta, enhances beta-catenin-dependent transcription by maintaining a high level of beta-catenin protein in the cytoplasm. More importantly, 14-3-3zeta facilitates activation of beta-catenin by the survival kinase Akt and colocalizes with activated Akt in intestinal stem cells. We propose that Akt phosphorylates beta-catenin, which results in 14-3-3zeta binding and stabilization of beta-catenin, and these interactions may be involved in stem cell development.