Abstract
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.
Original language | English (US) |
---|---|
Pages (from-to) | 225-233 |
Number of pages | 9 |
Journal | European journal of cell biology |
Volume | 84 |
Issue number | 2-3 |
DOIs | |
State | Published - Mar 9 2005 |
Funding
The author thanks former and present members of his lab for comments on the manuscript and especially Dr. J. Klingelhofer (Institute of Cancer Biology, Denmark) for help in preparing the figures. This work has been supported by Grant AR44016-04 from the National Institutes of Health.
Keywords
- Adhesion
- Cadherin
- Dimerization
ASJC Scopus subject areas
- Pathology and Forensic Medicine
- Histology
- Cell Biology