Cadherin-related family member 5 (CDHR5)

Cadherin-related family member 5 (CDHR5) is a cell surface, type-1 transmembrane protein and member of the cadherin superfamily, characterized by a mucin-like extracellular domain containing both tandem repeats and canonical cadherin calcium-binding motifs[2][5]. It mediates calcium-dependent heterophilic adhesion between microvilli, forming complexes with cadherin-related family member 2 (CDHR2), and organizes the packing and length of microvilli in epithelial cells such as those in the gut and kidney[1][2][3]. Its short cytoplasmic tail contains poly-proline motifs as well as a PDZ binding motif, enabling regulated interaction with cytoplasmic scaffolding proteins EBP50 and E3KARP, and thereby forming a molecular complex important for brush border assembly[1][5]. CDHR5 is encoded by a gene with multiple known splice isoforms and is subject to developmental regulation, tissue specificity, and altered expression in cancer and inflammation[1][2]. Loss of CDHR5 is noted in colorectal carcinomas, and it has been genetically linked to Usher syndrome type I[2]. Current research highlights its role in epithelial cell differentiation, microvillar structure and function, and as a potential biomarker or therapeutic target in diseases affecting epithelial integrity[1][2][3].

Other names

Mucin-like protocadherinMu-protocadherinMucin and cadherin-like proteinMUCDHLMUPCDHDifferentiation-associated catenin regulatorFLJ20219UNQ2781/PRO7168