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Neurite fasciculation mediated by complexes of axonin-1 and Ng cell adhesion molecule

Academic Article
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Overview

authors

  • Kunz, S.
  • Spirig, M.
  • Ginsburg, C.
  • Buchstaller, A.
  • Berger, P.
  • Lanz, R.
  • Rader, Christoph
  • Vogt, L.
  • Kunz, B.
  • Sonderegger, P.

publication date

  • December 1998

journal

  • Journal of Cell Biology  Journal

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.

subject areas

  • Animals
  • Animals, Newborn
  • Binding Sites
  • Cell Adhesion Molecules, Neuron-Glia
  • Cell Adhesion Molecules, Neuronal
  • Chickens
  • Contactin 2
  • Extracellular Space
  • Ganglia, Spinal
  • Mice
  • Mice, Inbred ICR
  • Models, Molecular
  • Mutagenesis
  • Neurites
  • Neurons
  • Organ Culture Techniques
  • Point Mutation
  • Polymerase Chain Reaction
  • Protein Conformation
  • Recombinant Proteins
  • Sequence Deletion
  • Transfection
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Research

keywords

  • axon guidance molecules
  • axonal fasciculation
  • cell adhesion molecules
  • cell contact
  • cell recognition
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Identity

International Standard Serial Number (ISSN)

  • 0021-9525

Digital Object Identifier (DOI)

  • 10.1083/jcb.143.6.1673

PubMed ID

  • 9852159
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Additional Document Info

start page

  • 1673

end page

  • 1690

volume

  • 143

issue

  • 6

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