| Analysis of heterophilic and homophilic interactions of cadherins using the c-Jun/c-Fos dimerization domains. | |
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MedLine Citation:
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PMID: 11909859 Owner: NLM Status: MEDLINE |
Abstract/OtherAbstract:
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Cadherin-mediated cell-cell adhesion is initiated by cis dimerization of cadherin ectodomains at the cell surface followed by an antiparallel trans interaction of dimers on opposing cells. To resolve open questions concerning the molecular details and specificity of cis and trans interactions, ectodomains of E- and P-cadherin were analyzed by chemical cross-linking and by electron microscopy. At the high intrinsic concentration created by artificial oligomerization the N-terminal cadherin (CAD)-domain of P-cadherin are forming ring-like cis dimers. At 2 mm Ca(2+)-associated rings involving two cis dimers indicate trans contacts in electron micrographs. cis and trans interactions were further analyzed by heterodimerization of the ectodomains of E-cadherin (ECAD) and P-cadherin (PCAD) through the leucine zipper domains of c-Jun and c-Fos. ECADJun/ECADFos dimers predominantly form ring-like cis dimers at 1 mm Ca(2+) and double-ringed trans contacts above 2 mm Ca(2+). The Ca(2+)-dependent tetrameric trans contacts of ECADJun/ECADFos dimers are also detectable after chemical cross-linking. Only cis contacts but no trans interactions are observed for heterodimers of ECADFos and the Trp-2 to Ala mutant ECADW2AJun arguing for a decisive role of Trp-2 in trans but not cis interaction. Neither cis nor trans interaction was found for heterodimers of ECADJun and PCADFos suggesting that specificity for homophilic interactions already exists at the level of cis dimerization. |
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Authors:
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Thomas Ahrens; Olivier Pertz; Daniel Haussinger; Charlotte Fauser; Therese Schulthess; Jurgen Engel |
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Publication Detail:
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Type: Journal Article; Research Support, Non-U.S. Gov't Date: 2002-03-21 |
Journal Detail:
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Title: The Journal of biological chemistry Volume: 277 ISSN: 0021-9258 ISO Abbreviation: J. Biol. Chem. Publication Date: 2002 May |
Date Detail:
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Created Date: 2002-05-28 Completed Date: 2002-07-02 Revised Date: 2006-11-15 |
Medline Journal Info:
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Nlm Unique ID: 2985121R Medline TA: J Biol Chem Country: United States |
Other Details:
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Languages: eng Pagination: 19455-60 Citation Subset: IM |
Affiliation:
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Department of Biophysical Chemistry, Biozentrum, University of Basel, Klingelbergstrasse 70, Basel 4056, Switzerland. |
Export Citation:
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| MeSH Terms | |
Descriptor/Qualifier:
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Animals Blotting, Western Cadherins / metabolism* Calcium / metabolism Cell Line Circular Dichroism Cross-Linking Reagents / pharmacology DNA, Complementary / metabolism Dimerization Humans Leucine / chemistry Mice Microscopy, Electron Protein Binding Protein Structure, Tertiary Proto-Oncogene Proteins c-fos / chemistry* Proto-Oncogene Proteins c-jun / chemistry* Signal Transduction Transfection |
| Chemical | |
Reg. No./Substance:
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0/Cadherins; 0/Cross-Linking Reagents; 0/DNA, Complementary; 0/Proto-Oncogene Proteins c-fos; 0/Proto-Oncogene Proteins c-jun; 61-90-5/Leucine; 7440-70-2/Calcium |
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine
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