| First Author | Vespa A | Year | 2005 |
| Journal | Mol Biol Cell | Volume | 16 |
| Issue | 9 | Pages | 4084-95 |
| PubMed ID | 15975904 | Mgi Jnum | J:104071 |
| Mgi Id | MGI:3611108 | Doi | 10.1091/mbc.E05-02-0087 |
| Citation | Vespa A, et al. (2005) A novel role for integrin-linked kinase in epithelial sheet morphogenesis. Mol Biol Cell 16(9):4084-95 |
| abstractText | 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 Ca(2+) triggers formation of cell-cell junctions, loss of focal adhesions, and ILK distribution to cell borders. We now show that Ca(2+) treatment of keratinocytes induces rapid (<or=1 h) translocation to the cell membrane of the adherens junction (AJ) proteins E-cadherin and beta-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/beta-catenin to cell borders, precluding Ca(2+)-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. |
