The raft-associated protein MAL is required for maintenance of proper axon–glia interactions in the central nervous system
| Autor: | Annick Bonnet, Udo Bartsch, Nicole Schaeren-Wiemers, Diane L. Sherman, Ned Mantei, Frances Kern, Beat Erne, Michael Erb, Ueli Suter |
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| Rok vydání: | 2004 |
| Předmět: |
Central Nervous System
Potassium Channels Proteolipid protein 1 Proteolipids Central nervous system Neural Conduction Down-Regulation Cell Communication Biology Article Mice Myelin Membrane Microdomains Compact myelin Ranvier's Nodes Kv1.2 Potassium Channel medicine Animals Nerve Growth Factors Axon Research Articles Myelin Sheath Mice Knockout Myelin-associated glycoprotein axon–glia interaction myelin proteolipids glycolipid-enriched microdomains node of Ranvier Myelin and Lymphocyte-Associated Proteolipid Proteins Membrane Transport Proteins Myelin Basic Protein Optic Nerve Cell Biology Sciatic Nerve Axons Transport protein Myelin basic protein Cell biology Microscopy Electron Myelin-Associated Glycoprotein Oligodendroglia Protein Transport medicine.anatomical_structure nervous system Potassium Channels Voltage-Gated Immunology biology.protein lipids (amino acids peptides and proteins) Cell Adhesion Molecules Myelin Proteins |
| Zdroj: | The Journal of Cell Biology |
| ISSN: | 1540-8140 0021-9525 |
| DOI: | 10.1083/jcb.200406092 |
| Popis: | 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. |
| Databáze: | OpenAIRE |
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