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First published online 25 January 2005
doi: 10.1242/jcs.01638
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Research Article |
1 Department of Pathology, Center for Biological Imaging, University of Pittsburgh, Pittsburgh, PA 15261, USA
2 Department of Cell Biology and Physiology, Center for Biological Imaging, University of Pittsburgh, Pittsburgh, PA 15261, USA
Author for correspondence (e-mail: carywu{at}pitt.edu)
Accepted 8 November 2004
Cell-cell junctions are essential for epithelial and endothelial tissue formation and communication between neighboring cells. We report here that migfilin, a recently identified component of cell-extracellular matrix adhesions, is recruited to cell-cell junctions in response to cadherin-mediated cell-cell adhesions. Migfilin is detected at cell-cell junctions in both epithelial and endothelial cells. It forms detergent-resistant, discrete clusters that associate with actin bundles bridging neighboring cells. Immunoelectron microscopic analyses reveal that migfilin is closely associated with ß-catenin, but not desmosomes, at cell-cell junctions. Furthermore, we show that the C-terminal LIM domains, but not its N-terminal domain, mediates migfilin localization to cell-cell junctions. The site mediating the localization of migfilin to cell-cell junctions at least partially overlaps with that mediating the localization of migfilin to cell-ECM adhesions. Finally, siRNA-mediated depletion of migfilin compromised the organization of adherens junctions and weakened cell-cell association. These results identify migfilin as a component of adherens junctions and suggest an important role for migfilin in the organization of the cell-cell adhesion structure.
Key words: Migfilin, Catenin, Mig-2, Cell-cell junctions, Cell-extracellular matrix adhesions, Actin cytoskeleton
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