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Description

Cadherin-5 (UniProt: P33151, also known as 7B4 antigen, Vascular endothelial cadherin, VE-cadherin, CD144) is encoded by the CDH5 gene (Gene ID: 1003) in human. Cadherins are calcium-dependent cell adhesion proteins, which preferentially interact with themselves in a homophilic manner in connecting cells. Cadherin 5 is a single-pass type I membrane protein that is found at cell-cell boundaries and may also be located at cell-matrix boundaries. It is well expressed in brain and endothelial tissue. It plays an important role in endothelial cell biology through control of the cohesion and organization of the intercellular junctions. It associates with alpha-catenin forming a link to the cytoskeleton. Cadherin 5 acts in concert with KRIT1 to establish and maintain correct endothelial cell polarity and vascular lumen. These effects are mediated by recruitment and activation of the Par polarity complex and RAP1B. Cadherin 5 is synthesized as a preproprotein with a signal peptide (aa 1-25) and propeptide (aa 26-47) that are proteolytically cleaved to produce the mature glycoprotein. It has an extracellular domain (aa 48-599), a short transmembrane domain (aa 600-620), and a cytoplasmic domain (aa 621-784) and contains five cadherin domains. Three calcium ions are usually bound at the interface of each cadherin domain and rigidify the connections, providing a strong curvature to the full-length ectodomains. Two isoforms of Cadherin 5 have been described that are produced by alternative splicing. Cadherin 5 can be phosphorylated on tyrosine residues by KDR/VRGFR-2. Phosphorylation at Tyr731 leads to the separation of beta-catenin from the cytoplasmic tail Cadherin 5. This phosphorylation event reported to be sufficient to maintain cells in a mesenchymal state during the cell invasion phase of angiogenesis.