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Axonin-1/TAG-1 mediates cell-cell adhesion by a cis-assisted trans-interaction

Academic Article
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Overview

authors

  • Kunz, B.
  • Lierheimer, R.
  • Rader, Christoph
  • Spirig, M.
  • Ziegler, U.
  • Sonderegger, P.

publication date

  • February 2002

journal

  • Journal of Biological Chemistry  Journal

abstract

  • The neural cell adhesion molecule axonin-1/TAG-1 mediates cell-cell interactions via homophilic and heterophilic contacts. It consists of six Ig and four fibronectin type III domains anchored to the membrane by glycosylphosphatidylinositol. The recently solved crystal structure indicates a module composed of the four N-terminal Ig domains as the contact site between trans-interacting axonin-1 molecules from apposed membranes. Here, we have tested domain-specific monoclonal antibodies for their capacity to interfere with homophilic binding in a cell aggregation assay. The results confirmed the existence of a binding region within the N-terminal Ig domains and identified a second region contributing to homophilic binding on the third and fourth fibronectin domains near the C terminus. The perturbation of each region alone resulted in a complete loss of cell aggregation, suggesting that axonin-1-mediated cell-cell contact results from a cooperative action of two homophilic binding regions. The data support that axonin-1-mediated cell-cell contact is formed by cis-assisted trans-binding. The N-terminal binding regions of axonin-1 establish a linear zipper-like string of trans-interacting axonin-1 molecules alternately provided by the two apposed membranes. The C-terminal binding regions strengthen the cell-cell contact by enhancing the expansion of the linear string into a two-dimensional array via cis-interactions. Cis-assisted trans-binding may be a basic binding mechanism common to many cell adhesion molecules.

subject areas

  • Animals
  • Cell Adhesion
  • Cell Adhesion Molecules, Neuronal
  • Cell Line
  • Chick Embryo
  • Contactin 2
  • Mice
  • Mice, Inbred BALB C
  • Protein Binding
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Identity

International Standard Serial Number (ISSN)

  • 0021-9258

Digital Object Identifier (DOI)

  • 10.1074/jbc.M109779200

PubMed ID

  • 11733523
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Additional Document Info

start page

  • 4551

end page

  • 4557

volume

  • 277

issue

  • 6

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