Cadherin dimers in cell-cell adhesion

Eur J Cell Biol. 2005 Mar;84(2-3):225-33. doi: 10.1016/j.ejcb.2004.12.009.


While the critical function of classic cadherin in cell-cell junctions is well established, the molecular mechanism of cadherin-based adhesion remains unclear. The elusive but principal part of this adhesion process is the cadherin-cadherin interaction maintaining the intercellular contacts. This interaction is believed to be weak, suggesting that the adhesive contacts are strengthened by the cytoskeleton-dependent clustering of numerous cadherin molecules. An examination of cadherin homodimers in living cells has shown, however, that cadherin adhesive interaction is surprisingly strong. This observation implies that the strength of the adhesive contacts is regulated by the processes disintegrating cadherin dimers. The molecular structure of these dimers and mechanisms potentially responsible for their dynamics in living cells are discussed in this review.

Publication types

  • Research Support, N.I.H., Extramural
  • Research Support, U.S. Gov't, P.H.S.
  • Review

MeSH terms

  • Animals
  • Cadherins / physiology*
  • Calcium / physiology
  • Cell Adhesion / physiology
  • Dimerization
  • Humans


  • Cadherins
  • FAT1 protein, human
  • Calcium