The PDZ Protein Erbin Modulates β-Catenin-Dependent Transcription
Autor: | K. Moelling, A. Ress |
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Rok vydání: | 2008 |
Předmět: |
Beta-catenin
Transcription Genetic PDZ domain PDZ Domains Ligands Transfection Models Biological Receptor tyrosine kinase Cell Line Genes Reporter Transcription (biology) Humans Luciferases Protein kinase A Cell adhesion beta Catenin Adaptor Proteins Signal Transducing Sequence Deletion Binding Sites biology Chemistry Activator (genetics) Wnt signaling pathway Recombinant Proteins Cell biology Mutation Cancer research biology.protein Surgery Signal Transduction |
Zdroj: | European Surgical Research. 41:284-289 |
ISSN: | 1421-9921 0014-312X |
DOI: | 10.1159/000148241 |
Popis: | Erbin is a member of the leucine-rich repeat and PDZ domain family that can regulate proliferation, differentiation and cell adhesion. As a binding partner of the receptor tyrosine kinase ErbB2, erbin targets this receptor to the basolateral membrane of polarized epithelial cells. In addition, erbin is known to inhibit the Ras-mediated activation of the mitogen-activated protein kinase pathway. Recently we identified the proto-oncoprotein β-catenin as a ligand of the PDZ domain of erbin. Here we demonstrate that erbin acts as a negative regulator of the β-catenin/T-cell-factor-dependent gene expression. In contrast, a mutant of erbin with a deletion of the N-terminal leucine-rich repeat allows the PDZ domain of erbin to increase the β-catenin/T-cell-factor-dependent transcription. This mutant localizes to the nucleus and mimics a putative splice variant found in keratinocytes. Thus, erbin has the potential to act as an inhibitor as well as an activator of the β-catenin-regulated gene expression. |
Databáze: | OpenAIRE |
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