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


  • C. Hogan
  • N. Serpente
  • P. Cogram
  • C.R. Hosking
  • C.U. Bialucha
  • S.M. Feller
  • V.M.M. Braga
  • W. Birchmeier
  • Y. Fujita


  • Molecular and Cellular Biology


  • Mol Cell Biol 24 (15): 6690-6700


  • 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.