A Novel Role for Integrin-linked Kinase in Epithelial Sheet Morphogenesis
Autor: | Lina Dagnino, Alisa Vespa, Sudhir J.A. D'Souza |
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Rok vydání: | 2005 |
Předmět: |
Keratinocytes
Cellular differentiation Morphogenesis Motility Protein Serine-Threonine Kinases Epithelium Tight Junctions Adherens junction Focal adhesion Mice Animals Integrin-linked kinase Fluorescent Antibody Technique Indirect Molecular Biology Cells Cultured biology Kinase Cell Differentiation Adherens Junctions Articles Cell Biology Ankyrin Repeat Cell biology Transport protein Kinetics Protein Transport Mutation embryonic structures biology.protein |
Zdroj: | Molecular Biology of the Cell. 16:4084-4095 |
ISSN: | 1939-4586 1059-1524 |
DOI: | 10.1091/mbc.e05-02-0087 |
Popis: | Integrin-linked kinase (ILK) is a multidomain protein involved in cell motility and cell-extracellular matrix interactions. ILK is found in integrin-containing focal adhesions in undifferentiated primary epidermal keratinocytes. Induction of keratinocyte differentiation by treatment with Ca2+triggers formation of cell–cell junctions, loss of focal adhesions, and ILK distribution to cell borders. We now show that Ca2+treatment of keratinocytes induces rapid (≤1 h) translocation to the cell membrane of the adherens junction (AJ) proteins E-cadherin and β-catenin. This is followed by slower (>6 h) localization of tight junction (TJ) proteins. The kinetics of ILK movement toward the cell periphery mimics that of AJ components, suggesting that ILK plays a role in the early formation of cell–cell contacts. Whereas the N terminus in ILK mediates localization to cell borders, expression of an ILK deletion mutant incapable of localizing to the cell membrane (ILK 191-452) interferes with translocation of E-cadherin/β-catenin to cell borders, precluding Ca2+-induced AJ formation. Cells expressing ILK 191-452 also fail to form TJ and sealed cell–cell borders and do not form epithelial sheets. Thus, we have uncovered a novel role for ILK in epithelial cell–cell adhesion, independent of its well-established role in integrin-mediated adhesion and migration. |
Databáze: | OpenAIRE |
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