Rap1 regulates the formation of E-cadherin-based cell-cell contacts |
| |
Authors: | Hogan Catherine Serpente Norberto Cogram Patricia Hosking Catherine Rose Bialucha Carl Uli Feller Stephan Michael Braga Vania M M Birchmeier Walter Fujita Yasuyuki |
| |
Institution: | MRC Laboratory for Molecular Cell Biology and Cell Biology Unit, University College London, Gower Street, London WC1E 6BT, United Kingdom. |
| |
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: | |
本文献已被 PubMed 等数据库收录! |
|