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

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.

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Item Permalink: http://hdl.handle.net/11858/00-001M-0000-0010-6CCE-1 Version Permalink: http://hdl.handle.net/11858/00-001M-0000-0010-6CCF-0
Genre: Journal Article
Alternative Title : J. Mol. Biol.

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 Creators:
Ahrens, T., Author
Lambert, M., Author
Pertz, O., Author
Sasaki, T.1, Author              
Schulthess, T., Author
Mege, R. M., Author
Timpl, R.1, Author              
Engel, J., Author
Affiliations:
1Former Research Groups, Max Planck Institute of Biochemistry, Max Planck Society, ou_1565145              

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Free keywords: VE-cadherin; N-cadherin; oligomerization domains; homoassociation; cell adhesion
 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

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Language(s): eng - English
 Dates: 2003-01-24
 Publication Status: Published in print
 Pages: -
 Publishing info: -
 Table of Contents: -
 Rev. Method: Peer
 Identifiers: eDoc: 41687
ISI: 000180544800011
 Degree: -

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Title: Journal of Molecular Biology
  Alternative Title : J. Mol. Biol.
Source Genre: Journal
 Creator(s):
Affiliations:
Publ. Info: -
Pages: - Volume / Issue: 325 (4) Sequence Number: - Start / End Page: 733 - 742 Identifier: ISSN: 0022-2836