1. Rap1 Regulates the Formation of E-Cadherin-Based Cell-Cell Contacts.
- Author
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Hogan, Catherine, Serpente, Norberto, Cogram, Patricia, Hosking, Catherine Rose, Bialucha, Carl Uli, Feller, Stephan Michael, Braga, Vania M.M., Birchmeier, Walter, and Fujita, Yasuyuki
- Subjects
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CELL communication , *EPITHELIAL cells , *PROTEINS , *CYTOPLASM , *CELL adhesion , *MEMBRANE proteins - Abstract
In epithelial tissues, cells are linked to their neighbors through specialized cell-cell adhesion proteins. E-cadherin is one of the most important membrane proteins for the establishment of intimate cell-cell contacts, but the molecular mechanism by which it is recruited to contact sites is largely unknown. We report here that the cytoplasmic domain of E-cadherin interacts with C3G, a guanine nucleotide exchange factor for Rap1. In epithelial cell cultures, ligation of the extracellular domain of E-cadherin enhances Rap1 activity, which in turn is necessary for the proper targeting of E-cadherin molecules to maturing cell-cell contacts. Furthermore, our data suggest that Cdc42 functions downstream of Rap1 in this process. We conclude that Rap1 plays a vital role in the establishment of E-cadherin-based cell-cell adhesion. [ABSTRACT FROM AUTHOR]
- Published
- 2004
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