Authors
Creative Biogene
Summary
Cadherins constitute a large superfamily of cell surface receptors, many of which function in calcium-dependent cell-cell recognition and adhesion. Cadherins are found in a wide array of species ranging from unicellular animals with multicellular life stages to mammals, in which they are involved in morphogenetic processes such as embryonic cell layer separation, cell signaling, synapse formation and specificity in the central nervous system, mechanotransduction, and physical homeostasis of mature tissues. Consistent with these roles, decreased cadherin expression, which may allow cells to escape normal viability requirements for cellular cohesion, is a common feature of metastasis.
Introduction
Members of the cadherin superfamily are defined by a common structural component, the EC domain – an about 110 residues β-fold domain – and cadherins can be classified into multiple subfamilies based on the number and arrangement of EC domains. By far the best understood of these subfamilies are the vertebrate classical cadherins, comprising six ‘type I’ and 13 ‘type II’ cadherins in typical vertebrate genomes, which share a conserved cytoplasmic domain and an ectodomain containing five tandem EC domains. Linkers between successive EC domains are each stabilized by the binding of three Ca2+ ions leading to a characteristic curvature of the ectodomai.
Materials
Classical cadherins provide the prototypical example of calcium-dependent homophilic cell-cell adhesion. They are often concentrated at adherens junctions, specialized cell-cell adhesion structures characterized by parallel apposed plasma membranes with an intermembrane space of approximately 15–30 nm. In these junctions, cadherins form trans bonds bridging the intermembrane space by their ectodomains, while their cytoplasmic domains bind to the adaptor proteins β-catenin, which links cadherins indirectly to the cytoskeleton, and p120 catenin which regulates cadherin turnover and modulates actin assembly.
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