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J Cell Biol ; 143(6): 1673-90, 1998 Dec 14.
Article in English | MEDLINE | ID: mdl-9852159

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(s)
Cell Adhesion Molecules, Neuron-Glia/chemistry , Cell Adhesion Molecules, Neuron-Glia/physiology , Cell Adhesion Molecules, Neuronal/chemistry , Cell Adhesion Molecules, Neuronal/physiology , Ganglia, Spinal/physiology , Neurites/physiology , Protein Conformation , Animals , Animals, Newborn , Binding Sites , Cell Adhesion Molecules, Neuron-Glia/genetics , Cell Adhesion Molecules, Neuronal/genetics , Chickens , Contactin 2 , Extracellular Space/physiology , Mice , Mice, Inbred ICR , Models, Molecular , Mutagenesis , Neurons/cytology , Neurons/physiology , Organ Culture Techniques , Point Mutation , Polymerase Chain Reaction , Recombinant Proteins/chemistry , Recombinant Proteins/metabolism , Sequence Deletion , Transfection
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