Ahrens T Lambert M Pertz O Sasaki T Schulthess T Mège RM Timpl R Engel J 2003 Vascular endothelial cadherin (VE-cadherin/cadherin5) is specifically expressed in adherens junctions of endothelial cells and exerts important functions in cell-cell adhesion as well as signal transduction. To analyze the mechanism of VE-cadherin homoassociation, the ectodomains CAD1-5 were connected by linker sequences to the N terminus of the coiled-coil domain of cartilage matrix protein (CMP). The chimera VECADCMP were expressed in mammalian cells. The trimeric coiled-coil domain leads to high intrinsic domain concentrations and multivalency promoting self-association. Ca(2+)-dependent homophilic association of VECADCMP was detected in solid phase assays and cross-linking experiments. A striking analogy to homoassociation of type I ("classical") cadherins like E, N or P-cadherin was observed when interactions in VECADCMP and between these trimeric proteins were analyzed by electron microscopy. Ca(2+)-dependent ring-like and double ring-like arrangements suggest interactions between domains 1 and 2 of the ectodomains, which may be correlated with lateral and adhesive contacts in the adhesion process. Association to complexes composed of two VECADCMP molecules was also demonstrated by chemical cross-linking. No indication for an antiparallel association of VECAD ectodomains to hexameric complexes as proposed by Legrand et al. was found. Instead the data suggest that homoassociation of VE-cadherin follows the conserved mechanism of type I cadherins. https://sonar.ch/global/documents/4648 eng info:eu-repo/semantics/altIdentifier/doi/10.1016/s0022-2836(02)01286-x info:eu-repo/semantics/altIdentifier/pmid/12507476 Journal of molecular biology. - 2003 Animals Antigens, CD Base Sequence Cadherins Calcium Cell Adhesion Cell Line Chickens Cross-Linking Reagents DNA, Complementary Humans Mice Microscopy, Electron Protein Structure, Quaternary Protein Structure, Tertiary Recombinant Fusion Proteins Homoassociation of VE-cadherin follows a mechanism common to "classical" cadherins. http://purl.org/coar/resource_type/c_6501