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Published online 15 December 2003. doi:10.1083/jcb.200309147
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© The Rockefeller University Press, 0021-9525/2003/12/1213 $8.00
The Journal of Cell Biology, Volume 163, Number 6, 1213-1218

Report

Caspr regulates the processing of contactin and inhibits its binding to neurofascin



Leora Gollan1, Daniela Salomon1, James L. Salzer2 and Elior Peles1

1 Department of Molecular Cell Biology, The Weizmann Institute of Science, Rehovot 76100 Israel
2 Department of Cell Biology and Neurology, Program in Molecular Neurobiology, Skirball Institute of Biomedical Research, New York University School of Medicine, New York, NY 10016

Address correspondence to Elior Peles, Department of Molecular Cell Biology, The Weizmann Institute of Science, Rehovot 76100 Israel. Tel.: 972-8-934-2941. Fax: 972-8-934-4195. email: peles{at}weizmann.ac.il

Three cell adhesion molecules are present at the axoglial junctions that form between the axon and myelinating glia on either side of nodes of Ranvier. These include an axonal complex of contacin-associated protein (Caspr) and contactin, which was proposed to bind NF155, an isoform of neurofascin located on the glial paranodal loops. Here, we show that NF155 binds directly to contactin and that surprisingly, coexpression of Caspr inhibits this interaction. This inhibition reflects the association of Caspr with contactin during biosynthesis and the resulting expression of a low molecular weight (LMw), endoglycosidase H–sensitive isoform of contactin at the cell membrane, which remains associated with Caspr but is unable to bind NF155. Accordingly, deletion of Caspr in mice by gene targeting results in a shift from the LMw- to a HMw-contactin glycoform. These results demonstrate that Caspr regulates the intracellular processing and transport of contactin to the cell surface, thereby affecting its ability to interact with other cell adhesion molecules.

Key Words: node of Ranvier; transport; cell adhesion; paranodal junction; myelin

Abbreviations used in this paper: Caspr, contacin-associated protein; EndoH, endoglycosidase H; HMw, high molecular weight; LMw, low molecular weight.


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