E-cadherin (green) contacts dissolve when uPAR and α3β1 interact (right).

On page 177, Zhang et al. show that the extracellular domain of the α3β1 integrin can hijack a glycolipid- anchored receptor and thus trigger movement of an epithelial cell by inhibiting E-cadherin–mediated cell contacts.

Integrins on epithelial cells are well known to tether the cells to matrix components—laminin-5 in the case of α3β1—but are not usually associated with cell–cell contacts. Zhang et al. show that α3β1 can inhibit cell–cell contacts when α3 binds to the urokinase receptor, uPAR, a known inducer of cell migration in response to certain cytokines. Expression of both uPAR and α3β1 mobilized cells by reducing E-cadherin and γ-catenin levels at cell junctions, thus dissociating the cells. Other uPAR-induced changes included expression of several genes that are associated with the epithelial–mesenchymal transition, such as the transcription factor SLUG....

The Rockefeller University Press
2003
The Rockefeller University Press
2003
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