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Implications for the domain arrangement of axonin-1 derived from the mapping of its NgCAM binding site

Academic Article
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Overview

authors

  • Rader, Christoph
  • Kunz, B.
  • Lierheimer, R.
  • Giger, R. J.
  • Berger, P.
  • Tittmann, P.
  • Gross, H.
  • Sonderegger, P.

publication date

  • 1996

journal

  • EMBO Journal  Journal

abstract

  • 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.

subject areas

  • Animals
  • Base Sequence
  • Binding Sites
  • Cell Adhesion Molecules, Neuron-Glia
  • Cell Adhesion Molecules, Neuronal
  • Cell Line
  • Chick Embryo
  • Contactin 2
  • Microscopy, Electron
  • Molecular Sequence Data
  • Neurites
  • Oligodeoxyribonucleotides
  • Protein Binding
  • Protein Folding
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Research

keywords

  • NgCAM
  • axonin-1
  • domain arrangement
  • immunoglobulin superfamily
  • neuronal cell adhesion molecules
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Identity

PubMed Central ID

  • PMC450127

International Standard Serial Number (ISSN)

  • 0261-4189

PubMed ID

  • 8641271
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Additional Document Info

start page

  • 2056

end page

  • 2068

volume

  • 15

issue

  • 9

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