cadherintype

Cadherin-type proteins, often referred to as cadherins, constitute a large superfamily of calcium-dependent transmembrane glycoproteins that mediate cell–cell adhesion in animal tissues. They function primarily through homophilic interactions, whereby cadherin molecules on neighboring cells bind to each other to hold cells together and to drive tissue organization.

Structurally, classical cadherins are single-pass transmembrane proteins with a large extracellular region containing typically five conserved cadherin repeats (EC1–EC5). The extracellular domains mediate calcium-dependent adhesive binding, while the cytoplasmic tail recruits catenin adaptor proteins (such as β-catenin and p120-catenin) that link the cadherin complex to the actin cytoskeleton, stabilizing cell junctions and enabling dynamic remodeling.

Cadherins are broadly classified into classical cadherins—such as E-cadherin, N-cadherin, and P-cadherin—and non-classical cadherins, which include a variety of vertebrate cadherins with diverse functions. Desmosomal cadherins (desmogleins and desmocollins) form desmosomes that provide strong intercellular adhesion in tissues subjected to mechanical stress. Protocadherins and other atypical cadherins contribute to specialized adhesion in the nervous system and other contexts.

Functionally, cadherin-mediated adhesion is essential for tissue morphogenesis, maintenance of tissue architecture, and cellular sorting during development. Regulation of cadherin expression and function influences processes such as epithelial–mesenchymal transition, wound healing, and synaptic organization.

Clinical relevance arises from altered cadherin expression or function in disease. Loss of E-cadherin is linked to cancer progression and metastasis, while abnormal cadherin signaling can affect neural development and tissue integrity.