Phosphorylation of beta-catenin by AKT promotes beta-catenin transcriptional activity.
Increased transcriptional activity of beta-catenin resulting from Wnt/Wingless-dependent or -independent signaling has been detected in many types of human cancer, but the underlying mechanism of Wnt-independent regulation is poorly understood. We have demonstrated that AKT, which is activated downstream from epidermal growth factor receptor signaling, phosphorylates beta-catenin at Ser552 in ... vitro and in vivo. AKT-mediated phosphorylation of beta-catenin causes its disassociation from cell-cell contacts and accumulation in both the cytosol and the nucleus and enhances its interaction with 14-3-3zeta via a binding motif containing Ser552. Phosphorylation of beta-catenin by AKT increases its transcriptional activity and promotes tumor cell invasion, indicating that AKT-dependent regulation of beta-catenin plays a critical role in tumor invasion and development.
Mesh Terms:
14-3-3 Proteins, Amino Acid Sequence, Animals, Cell Line, Cell Nucleus, Cricetinae, Cricetulus, Cytosol, Humans, Molecular Sequence Data, Neoplasm Invasiveness, Neoplasms, Phosphorylation, Phosphoserine, Protein Binding, Protein Transport, Proto-Oncogene Proteins c-akt, Trans-Activators, Transcription, Genetic, beta Catenin
14-3-3 Proteins, Amino Acid Sequence, Animals, Cell Line, Cell Nucleus, Cricetinae, Cricetulus, Cytosol, Humans, Molecular Sequence Data, Neoplasm Invasiveness, Neoplasms, Phosphorylation, Phosphoserine, Protein Binding, Protein Transport, Proto-Oncogene Proteins c-akt, Trans-Activators, Transcription, Genetic, beta Catenin
J. Biol. Chem.
Date: Apr. 13, 2007
PubMed ID: 17287208
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