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.
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.
|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|
|Date:||14 December 1998|
|Deposited On:||11 Feb 2008 13:20|
|Last Modified:||27 Nov 2013 21:08|
|Publisher:||Rockefeller University Press|
|Funders:||Swiss National Science Foundation, Biotechnology Program of the European Commission|
|Citations:||Web of Science®. Times Cited: 75|
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