Journal
JOURNAL OF CELL SCIENCE
Volume 118, Issue 4, Pages 697-710Publisher
COMPANY BIOLOGISTS LTD
DOI: 10.1242/jcs.01638
Keywords
migfilin; catenin; Mig-2; cell-cell junctions; cell-extracellular; matrix adhesions; actin cytoskeleton
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Funding
- NCI NIH HHS [CA76541] Funding Source: Medline
- NIDDK NIH HHS [DK54639] Funding Source: Medline
- NIGMS NIH HHS [GM65188] Funding Source: Medline
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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 beta-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.
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