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

Hogan, Catherine, Serpente, N., Cogram, P., Hosking, C. R., Bialucha, C. U., Feller, S. M., Braga, V. M. M., Birchmeier, W. and Fujita, Y. 2004. Rap1 regulates the formation of E-Cadherin-based cell-cell contacts. Molecular and Cellular Biology 24 (15) , pp. 6690-6700. 10.1128/MCB.24.15.6690-6700.2004

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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.

Item Type: Article
Date Type: Publication
Status: Published
Schools: Biosciences
European Cancer Stem Cell Research Institute (ECSCRI)
Publisher: American Society for Microbiology
ISSN: 0270-7306
Last Modified: 04 Jun 2017 06:39
URI: http://orca.cf.ac.uk/id/eprint/63371

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