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Published 15 September 2003. doi:10.1083/jcb.200305078
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© The Rockefeller University Press, 0021-9525/2003/9/1161 $5.00
The Journal of Cell Biology, Volume 162, Number 6, 1161-1172

Article

 Association of TAG-1 with Caspr2 is essential for the molecular organization of juxtaparanodal regions of myelinated fibers

Maria Traka1, Laurence Goutebroze2, Natalia Denisenko2, Maria Bessa1, Artemisia Nifli1, Sophia Havaki3, Yoichiro Iwakura4, Fumihiko Fukamauchi5, Kazutada Watanabe6, Betty Soliven7, Jean-Antoine Girault2 and Domna Karagogeos1

1 Department of Basic Science, University of Crete Medical School and Institute of Molecular Biology and Biotechnology (IMBB), 71110 Heraklion, Greece
2 Institut National de la Santé et de la Recherche Medicale U 536, Université Pierre et Marie Curie (UPMC), Institut du Fer à Moulin, 75005 Paris, France
3 Neurobiology Research Institute, Cozzika Foundation, 11528 Athens, Greece
4 Center for Experimental Medicine, Institute of Medical Science, University of Tokyo, 108-8639 Tokyo, Japan
5 Department of Molecular Medical Science, Medical Research Institute, Tokyo Medical and Dental University, Tokyo and Tsukuba College of Technology, 305-005 Ibaraki, Japan
6 Department of BioEngineering, Nagaoka University of Technology, 940-21 Nagaoka, Japan
7 Department of Neurology, University of Chicago, Chicago, IL 60637

Address correspondence to Domna Karagogeos, Institute of Molecular Biology and Biotechnology, P.O. Box 1527, Vassilika Vouton, Heraklion 711 10, Crete, Greece. Tel.: 30-28-81-39-45-42. Fax: 30-28-81-39-45-30. email: karagoge{at}nefeli.imbb.forth.gr

Myelination results in a highly segregated distribution of axonal membrane proteins at nodes of Ranvier. Here, we show the role in this process of TAG-1, a glycosyl-phosphatidyl-inositol–anchored cell adhesion molecule. In the absence of TAG-1, axonal Caspr2 did not accumulate at juxtaparanodes, and the normal enrichment of shaker-type K+ channels in these regions was severely disrupted, in the central and peripheral nervous systems. In contrast, the localization of protein 4.1B, an axoplasmic partner of Caspr2, was only moderately altered. TAG-1, which is expressed in both neurons and glia, was able to associate in cis with Caspr2 and in trans with itself. Thus, a tripartite intercellular protein complex, comprised of these two proteins, appears critical for axo–glial contacts at juxtaparanodes. This complex is analogous to that described previously at paranodes, suggesting that similar molecules are crucial for different types of axo–glial interactions.

Key Words: TAG-1/axonin-1/contactin-2; paranodin/Caspr/NCP-1; potassium channels; protein 4.1B; nodes of Ranvier

M. Traka and L. Goutebroze contributed equally to this work.

M. Traka's present address is Department of Neurology, University of Chicago, 5841 South Maryland Ave., MC2030, Chicago, IL 60637-1470.

Abbreviations used in this paper: CMAP, compound muscle action potential; CNS, central nervous system; GPI, glycosylphosphatidylinositol; IB, immunoblot; IF, immunofluorescence; IgSF, Ig superfamily; IP, immunoprecipitation; IR, immunoreactivity; MAG, myelin-associated glycoprotein; NCP, neurexin IV-caspr-paranodin; P8, postnatal day 8; PNS, peripheral nervous system.


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