Journal
JOURNAL OF CELL BIOLOGY
Volume 163, Issue 6, Pages 1213-1218Publisher
ROCKEFELLER UNIV PRESS
DOI: 10.1083/jcb.200309147
Keywords
node of Ranvier; transport; cell adhesion; paranodal junction; myelin
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Funding
- NINDS NIH HHS [NS43474, R01 NS043474] Funding Source: Medline
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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.
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