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© The Rockefeller University Press, 0021-9525/2002/6/1247 $5.00
The Journal of Cell Biology, Volume 157, Number 7, June 24, 2002 1247-1256

Retention of a cell adhesion complex at the paranodal junction requires the cytoplasmic region of Caspr

¹ Department of Molecular Cell Biology, The Weizmann Institute of Science, Rehovot 76100, Israel
² The Burnham Institute, Neurobiology Program, La Jolla, CA 92037

Address correspondence to Dr. Elior Peles, Department of Molecular Cell Biology, The Weizmann Institute of Science, Rehovot 76100, Israel. Tel.: 97-28-934-2941. Fax: 97-28-934-4125. E-mail: peles{at}weizmann.ac.il

An axonal complex of cell adhesion molecules consisting of Caspr and contactin has been found to be essential for the generation of the paranodal axo-glial junctions flanking the nodes of Ranvier. Here we report that although the extracellular region of Caspr was sufficient for directing it to the paranodes in transgenic mice, retention of the Caspr–contactin complex at the junction depended on the presence of an intact cytoplasmic domain of Caspr. Using immunoelectron microscopy, we found that a Caspr mutant lacking its intracellular domain was often found within the axon instead of the junctional axolemma. We further show that a short sequence in the cytoplasmic domain of Caspr mediated its binding to the cytoskeleton-associated protein 4.1B. Clustering of contactin on the cell surface induced coclustering of Caspr and immobilized protein 4.1B at the plasma membrane. Furthermore, deletion of the protein 4.1B binding site accelerated the internalization of a Caspr–contactin chimera from the cell surface. These results suggest that Caspr serves as a "transmembrane scaffold" that stabilizes the Caspr/contactin adhesion complex at the paranodal junction by connecting it to cytoskeletal components within the axon.

Key Words: axon; node of Ranvier; myelin; axo-glia junction; protein 4.1

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