Rap1 regulates the formation of E-cadherin-based cell-cell contacts

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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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