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

Hogan, Catherine ORCID: https://orcid.org/0000-0002-1012-0896, 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:	27 Oct 2022 08:46
URI:	https://orca.cardiff.ac.uk/id/eprint/63371

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