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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
 

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

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.[1]

References

  1. Rap1 regulates the formation of E-cadherin-based cell-cell contacts. Hogan, C., Serpente, N., Cogram, P., Hosking, C.R., Bialucha, C.U., Feller, S.M., Braga, V.M., Birchmeier, W., Fujita, Y. Mol. Cell. Biol. (2004) [Pubmed]
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