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Permanent URL to this publication: http://dx.doi.org/10.5167/uzh-1070

Kunz, S; Spirig, M; Ginsburg, C; Buchstaller, A; Berger, P; Lanz, R; Rader, C; Vogt, L; Kunz, B; Sonderegger, P (1998). Neurite fasciculation mediated by complexes of axonin-1 and Ng cell adhesion molecule. Journal of Cell Biology, 143(6):1673-1690.

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Abstract

Neural cell adhesion molecules composed of immunoglobulin and fibronectin type III-like domains have been implicated in cell adhesion, neurite outgrowth, and fasciculation. Axonin-1 and Ng cell adhesion molecule (NgCAM), two molecules with predominantly axonal expression exhibit homophilic interactions across the extracellular space (axonin- 1/axonin-1 and NgCAM/NgCAM) and a heterophilic interaction (axonin-1-NgCAM) that occurs exclusively in the plane of the same membrane (cis-interaction). Using domain deletion mutants we localized the NgCAM homophilic binding in the Ig domains 1-4 whereas heterophilic binding to axonin-1 was localized in the Ig domains 2-4 and the third FnIII domain. The NgCAM-NgCAM interaction could be established simultaneously with the axonin-1-NgCAM interaction. In contrast, the axonin-1-NgCAM interaction excluded axonin-1/axonin-1 binding. These results and the examination of the coclustering of axonin-1 and NgCAM at cell contacts, suggest that intercellular contact is mediated by a symmetric axonin-12/NgCAM2 tetramer, in which homophilic NgCAM binding across the extracellular space occurs simultaneously with a cis-heterophilic interaction of axonin-1 and NgCAM. The enhanced neurite fasciculation after overexpression of NgCAM by adenoviral vectors indicates that NgCAM is the limiting component for the formation of the axonin-12/NgCAM2 complexes and, thus, neurite fasciculation in DRG neurons.

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Additional indexing

Item Type:Journal Article, refereed
Communities & Collections:04 Faculty of Medicine > Department of Biochemistry
07 Faculty of Science > Department of Biochemistry
DDC:570 Life sciences; biology
Language:English
Date:14 December 1998
Deposited On:11 Feb 2008 12:20
Last Modified:27 Nov 2013 20:08
Publisher:Rockefeller University Press
ISSN:0021-9525
Funders:Swiss National Science Foundation, Biotechnology Program of the European Commission
Publisher DOI:10.1083/jcb.143.6.1673
Related URLs:http://www.jcb.org/cgi/content/full/143/6/1673
PubMed ID:9852159

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