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Homoassociation of VE-cadherin follows a mechanism common to "classical" cadherins

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http://pubman.mpdl.mpg.de/cone/persons/resource/persons78606

Sasaki,  T.
Former Research Groups, Max Planck Institute of Biochemistry, Max Planck Society;

http://pubman.mpdl.mpg.de/cone/persons/resource/persons78797

Timpl,  R.
Former Research Groups, Max Planck Institute of Biochemistry, Max Planck Society;

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Citation

Ahrens, T., Lambert, M., Pertz, O., Sasaki, T., Schulthess, T., Mege, R. M., et al. (2003). Homoassociation of VE-cadherin follows a mechanism common to "classical" cadherins. Journal of Molecular Biology, 325(4), 733-742.


Cite as: http://hdl.handle.net/11858/00-001M-0000-0010-6CCE-1
Abstract
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"-dependent homophilic association of VECADCMP was detected in solid phase assays and crosslinking experiments. A striking analogy to homoassociation of type 1 ("classical") cadherins like E, N or P-cadherin was observed when interactions in VECADCMP and between these trimeric proteins were analyzed by electron microscopy. Ca2+- 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. (C) 2003 Elsevier Science Ltd. All rights reserved