Abstract
Cadherins constitute a superfamily of cell-cell adhesion molecules expressed in many different cell types that are required for proper cellular function and maintenance of tissue architecture. Classical cadherins are the best understood class of cadherins. They are single membrane spanning proteins with a divergent extracellular domain of five repeats and a conserved cytoplasmic domain. Binding between cadherin extracellular domains is weak, but strong cell-cell adhesion develops during lateral clustering of cadherins by proteins that link the cadherin cytoplasmic domain to the actin cytoskeleton. Understanding how different regions of cadherins regulate cell-cell adhesion has been a major focus of study. Here, we examine evidence of the structure and function of the extracellular domain of classical cadherins in regard to the control of recognition and adhesive contacts between cadherins on opposing cell surfaces. Early experiments that focused on understanding the homotypic, Ca++-dependent characteristics of cadherin adhesion are discussed, and data supporting the widely accepted cis- and trans-dimer models of cadherins are analyzed.
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© 2004 Springer-Verlag
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Perez, T.D., Nelson, W.J. (2004). Cadherin Adhesion: Mechanisms and Molecular Interactions. In: Behrens, J., Nelson, W.J. (eds) Cell Adhesion. Handbook of Experimental Pharmacology, vol 165. Springer, Berlin, Heidelberg. https://doi.org/10.1007/978-3-540-68170-0_1
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DOI: https://doi.org/10.1007/978-3-540-68170-0_1
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