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Published 30 August 2004. doi:10.1083/jcb.200406092
The Rockefeller University Press, 0021-9525 $8.00
JCB, Volume 166, Number 5, 731-742
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Article

 The raft-associated protein MAL is required for maintenance of proper axon–glia interactions in the central nervous system

Nicole Schaeren-Wiemers1, Annick Bonnet2, Michael Erb1, Beat Erne1, Udo Bartsch3, Frances Kern1, Ned Mantei2, Diane Sherman4, and Ueli Suter2

1 Neurobiology, Department of Research, University Hospital Basel, 4056 Basel, Switzerland
2 Institute of Cell Biology, Department of Biology, Swiss Federal Institute of Technology, ETH-Hönggerberg, 8093 Zürich, Switzerland
3 Center for Molecular Neurobiology Hamburg (ZMNH) and Department of Ophthalmology, University of Hamburg, 20146 Hamburg, Germany
4 Center for Neuroscience Research, University of Edinburgh, Edinburgh EH9 1QH, Scotland, UK

Address correspondence to Nicole Schaeren-Wiemers, Neurobiology, Dept. of Research, University Hospital Basel, Pharmacenter, Klingelbergstr. 50, 4056 Basel, Switzerland. Tel.: (41) 61-267-15-41. Fax: (41) 61-267-16-28. email: Nicole.Schaeren-Wiemers{at}unibas.ch

The myelin and lymphocyte protein (MAL) is a tetraspan raft-associated proteolipid predominantly expressed by oligodendrocytes and Schwann cells. We show that genetic ablation of mal resulted in cytoplasmic inclusions within compact myelin, paranodal loops that are everted away from the axon, and disorganized transverse bands at the paranode–axon interface in the adult central nervous system. These structural changes were accompanied by a marked reduction of contactin-associated protein/paranodin, neurofascin 155 (NF155), and the potassium channel Kv1.2, whereas nodal clusters of sodium channels were unaltered. Initial formation of paranodal regions appeared normal, but abnormalities became detectable when MAL started to be expressed. Biochemical analysis revealed reduced myelin-associated glycoprotein, myelin basic protein, and NF155 protein levels in myelin and myelin-derived rafts. Our results demonstrate a critical role for MAL in the maintenance of central nervous system paranodes, likely by controlling the trafficking and/or sorting of NF155 and other membrane components in oligodendrocytes.

Key Words: axon–glia interaction; myelin proteolipids; glycolipid-enriched microdomains; node of Ranvier

N. Schaeren-Wiemers and A. Bonnet contributed equally to this paper.

A. Bonnet's present address is Kanzlei DF-MP, Munich, Germany.

Abbreviations used in this paper: Caspr, contactin-associated protein/paranodin; CGT, ceramide galactosyl transferase; CNS, central nervous system; DIG, detergent-insoluble glycolipid-enriched complex; GalC, galactosylceramide; KO, knockout; L-MAG, large myelin-associated glycoprotein isoform; MAG, myelin-associated glycoprotein; MAL, myelin and lymphocyte protein; MBP, myelin basic protein; MOG, myelin oligodendrocyte glycoprotein; NaCh, sodium channel; NF, neurofascin; PLP, proteolipid protein; PNS, peripheral nervous system; WT, wild type.


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