Nectin-4 (PVRL4) is a type I transmembrane glycoprotein which belongs to the nectin family of Ig superfamily proteins. It contains two Ig-like C2-type domains and one Ig-like V-type domain. PVRL4 seems to be involved in cell adhesion through trans-homophilic and-heterophilic interactions, the latter including specifically interactions with nectin-1. It does not act as receptor for alpha-herpesvirus entry into cells. It is predominantly expressed in placenta, the embryo and breast carcinoma. But it is not detected in normal breast epithelium. The soluble form is produced by proteolytic cleavage at the cell surface (shedding), probably by ADAM17. Mutations in this gene are the cause of ectodermal dysplasia-syndactyly syndrome type 1, an autosomal recessive disorder.
Nectin-4 (PVRL4) is a type I transmembrane glycoprotein which belongs to the nectin family of Ig superfamily proteins. It contains two Ig-like C2-type domains and one Ig-like V-type domain. PVRL4 seems to be involved in cell adhesion through trans-homophilic and -heterophilic interactions, the latter including specifically interactions with nectin-1. It does not act as receptor for alpha-herpesvirus entry into cells. It is predominantly expressed in placenta, the embryo and breast carcinoma. But it is not detected in normal breast epithelium. The soluble form is produced by proteolytic cleavage at the cell surface (shedding), probably by ADAM17. Mutations in this gene are the cause of ectodermal dysplasia-syndactyly syndrome type 1, an autosomal recessive disorder.
Nectin-4 (gene name PVRL4, poliovirus receptor-like 4) is a 66 kDa type I transmembrane glycoprotein belonging to the Nectin family of Ig superfamily proteins. The Latin word necto means “to connect”, indicating the role of nectins in Ca2+‑independent cell-cell adhesion. Nectin-4 forms homodimers in cis, followed by interactions in trans with Nectin-1 or -4. Human Nectin-4 mRNA is normally expressed in the placenta, especially in endothelial cells, while in the mouse it is found in the embryo, lung, testis and brain. Human Nectin-4 cDNA encodes 510 amino acids (aa), including a 31 aa signal sequence, a 318 aa extracellular domain (ECD), a 21 aa transmembrane segment (TM), and a 140 aa cytoplasmic region. Nectin ECDs contain three Ig-like domains: an N‑terminal V-type that mediates ligand binding, and two C2-type. One Nectin‑4 isoform lacks aa 412-436 in the cytoplasmic domain (1). In many human ductal breast or non-small cell lung carcinomas, Nectin‑4 is upregulated and a soluble 43 kDa form is found in the plasma. This form is generated from the membrane protein via the action of TACE/ADAM-17. The extracellular domain of human Nectin-4 shares 91%, 92%, 93%, 91% and 90% amino acid sequence homology with the corresponding regions of mouse, rat, canine, porcine and bovine Nectin-4, respectively. In forming adherens junctions, trans interactions of Nectin-4 initiate cell-cell interactions and recruit intracellular cadherins through afadin and other junctional proteins. These interactions organize the actin cytoskeleton, strengthen attachment to basement membrane and promote further cell-cell connections. In humans, mutation of Nectin-4 has been correlated with ectodermal dysplasia-syndactyly syndrome, indicating a role for Nectin-4 in human development.
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