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Permanent URL to this publication: http://dx.doi.org/10.5167/uzh-1097

Kunz, B; Lierheimer, R; Rader, C; Spirig, M; Ziegler, U; Sonderegger, P (2002). Axonin-1/TAG-1 mediates cell-cell adhesion by a cis-assisted trans-interaction. Journal of Biological Chemistry, 277(6):4551-4557.

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Abstract

The neural cell adhesion molecule axonin-1/TAG-1 mediates cell-cell interactions via homophilic and heterophilic contacts. It consists of six Ig and four fibronectin type III domains anchored to the membrane by glycosylphosphatidylinositol. The recently solved crystal structure indicates a module composed of the four N-terminal Ig domains as the contact site between trans-interacting axonin-1 molecules from apposed membranes. Here, we have tested domain-specific monoclonal antibodies for their capacity to interfere with homophilic binding in a cell aggregation assay. The results confirmed the existence of a binding region within the N-terminal Ig domains and identified a second region contributing to homophilic binding on the third and fourth fibronectin domains near the C terminus. The perturbation of each region alone resulted in a complete loss of cell aggregation, suggesting that axonin-1-mediated cell-cell contact results from a cooperative action of two homophilic binding regions. The data support that axonin-1-mediated cell-cell contact is formed by cis-assisted trans-binding. The N-terminal binding regions of axonin-1 establish a linear zipper-like string of trans-interacting axonin-1 molecules alternately provided by the two apposed membranes. The C-terminal binding regions strengthen the cell-cell contact by enhancing the expansion of the linear string into a two-dimensional array via cis-interactions. Cis-assisted trans-binding may be a basic binding mechanism common to many cell adhesion molecules.

Item Type:Journal Article, refereed
Communities & Collections:04 Faculty of Medicine > Institute of Biochemistry
07 Faculty of Science > Institute of Biochemistry
DDC:570 Life sciences; biology
Language:English
Date:08 February 2002
Deposited On:11 Feb 2008 13:20
Last Modified:27 Nov 2013 20:06
Publisher:American Society for Biochemistry and Molecular Biology
ISSN:0021-9258
Funders:Swiss National Science Foundation, Fonds für Medizinische Forschung der Universität Zürich, Julius Klaus-Stiftung, Sandoz-Stiftung, Olga Mayenfisch Stiftung, Jubiläumsstiftung der Rentenanstalt/Swiss Life.
Publisher DOI:10.1074/jbc.M109779200
PubMed ID:11733523
Citations:Web of Science®. Times Cited: 26
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