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| Item Type: | Article |
|---|---|
| Title: | Rap1 regulates the formation of E-cadherin-based cell-cell contacts |
| Creators Name: | Hogan, C., Serpente, N., Cogram, P., Hosking, C.R., Bialucha, C.U., Feller, S.M., Braga, V.M.M., Birchmeier, W. and Fujita, Y. |
| 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. |
| Keywords: | Binding Sites, Cadherins, Calcium, CDc42 GTP-Binding Protein, Cell Adhesion, Cell Communication, Cell Line, CHO Cells, Cricetinae, Cytoplasm, Epithelium, Guanine Nucleotide-Releasing Factor 2, Guanosine Triphosphate, Fluorescence Microscopy, Plasmids, Protein Binding, Rap1 GTP-Binding Proteins, Tertiary Protein Structure, Time Factors, Transfection, Tumor Cell Line, Two-Hybrid System Techniques, Western Blotting, Animals |
| Source: | Molecular and Cellular Biology |
| ISSN: | 0270-7306 |
| Publisher: | American Society for Microbiology |
| Volume: | 24 |
| Number: | 15 |
| Page Range: | 6690-6700 |
| Date: | 1 January 2004 |
| Official Publication: | https://doi.org/10.1128/MCB.24.15.6690-6700.2004 |
| PubMed: | View item in PubMed |
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