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© The Rockefeller University Press, 0021-9525/1998//1673 $5.00
The Journal of Cell Biology, Volume 143, Number 6, , 1998 1673-1690

Article

Neurite Fasciculation Mediated by Complexes of Axonin-1 and Ng Cell Adhesion Molecule



Stefan Kunz, Marianne Spirig, Claudia Ginsburg, Andrea Buchstaller, Philipp Berger, Rainer Lanz, Christoph Rader, Lorenz Vogt, Beat Kunz, and Peter Sonderegger

Institute of Biochemistry, University of Zurich, CH-8057 Zurich, Switzerland

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.

Key Words: axonal fasciculation • axon guidance molecules • cell adhesion molecules • cell contact • cell recognition

Abbreviations used in this paper: CAM, cell adhesion molecule; DRG, dorsal root ganglia; ECL, enhanced chemiluminescence; ECM, extracellular matrix; Fab, fragment with an antigen binding site; FnIII, fibronectin type-III; IgSF, immunoglobulin superfamily; IgFnIII, immunoglobulin/fibronectin type-III class of molecules; NBCS, newborn calf serum; pfu, plaque-forming unit.

Address all correspondence to Dr. Peter Sonderegger, Institute of Biochemistry, University of Zurich, Winterthurerstr. 190, CH-8057 Zurich, Switzerland. Tel.: 41 1 635 55 41. Fax: 41 1 635 68 31. E-mail: pson{at}bioc.uniz.ch


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