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Permanent URL to this publication: http://dx.doi.org/10.5167/uzh-1135

Rader, C; Kunz, B; Lierheimer, R; Giger, R J; Berger, P; Tittmann, P; Gross, H; Sonderegger, P (1996). Implications for the domain arrangement of axonin-1 derived from the mapping of its NgCAM binding site. The EMBO Journal, 15(9):2056-2068.



The neuronal cell adhesion molecule axonin-1 is composed of six immunoglobulin and four fibronectin type III domains. Axonin-1 promotes neurite outgrowth, when presented as a substratum for neurons in vitro, via a neuronal receptor that has been identified as the neuron-glia cell adhesion molecule, NgCAM, based on the blocking effect of polyclonal antibodies directed to NgCAM. Here we report the identification of axonin-1 domains involved in NgCAM binding. NgCAM-conjugated microspheres were tested for binding to COS cells expressing domain deletion mutants of axonin-1. In addition, monoclonal antibodies directed to axonin-1 were assessed for their ability to block the axonin-1-NgCAM interaction, and their epitopes were mapped using the domain deletion mutants. The results suggest that the four amino-terminal immunoglobulin domains of axonin-1 form a domain conglomerate which is necessary and sufficient for NgCAM binding. Surprisingly, NgCAM binding to membrane-bound axonin-1 was increased strongly by deletion of the fifth or sixth immunoglobulin domains of axonin-1. Based on these results and on negative staining electron microscopy, we propose a horseshoe-shaped domain arrangement of axonin-1 that obscures the NgCAM binding site. Neurite outgrowth studies with truncated forms of axonin-1 show that axonin-1 is a neurite outgrowth-promoting substratum in the absence of the NgCAM binding site.


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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
Dewey Decimal Classification:570 Life sciences; biology
Date:1 May 1996
Deposited On:11 Feb 2008 12:21
Last Modified:05 Apr 2016 12:17
Publisher:European Molecular Biology Organization ; Nature Publishing Group
Funders:Swiss National Science Foundation, Bonizzi-Theler-Stiftung, Sassella-Stiftung, Union Bank of Switzerland on behalf of a client.
Related URLs:http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pubmed&pubmedid=8641271
PubMed ID:8641271

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