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

Nicole Schaeren-Wiemers1, Annick Bonnet, Michael Erb

  • 1Neurobiology, Department of Research, University Hospital Basel, 4056 Basel, Switzerland. Nicole.Schaeren-Wiemers@unibas.ch

The Journal of Cell Biology
|September 1, 2004
PubMed

Insights

Genetic ablation of myelin and lymphocyte protein (MAL) disrupts central nervous system myelin structure and function. This protein is critical for maintaining paranodal integrity and proper protein localization in oligodendrocytes.

Area of Science:

  • Neuroscience
  • Cell Biology
  • Molecular Biology

Background:

  • Myelin and lymphocyte protein (MAL) is a proteolipid protein crucial for myelin sheath formation and maintenance.
  • It is predominantly expressed in oligodendrocytes and Schwann cells, forming tetraspan rafts.

Purpose of the Study:

  • To investigate the role of MAL in the structural integrity and protein composition of the central nervous system (CNS) paranodes.
  • To understand how MAL deficiency affects myelin structure and the localization of key paranodal proteins.

Main Methods:

  • Genetic ablation of the mal gene in adult mice.
  • Electron microscopy to analyze myelin and paranodal structure.
  • Biochemical analysis of myelin and myelin-derived rafts to assess protein levels.

Main Results:

  • Mice lacking MAL exhibited cytoplasmic inclusions in compact myelin and everted paranodal loops.
  • Significant reduction in contactin-associated protein/paranodin, neurofascin 155 (NF155), and Kv1.2 channels at paranodes.
  • Nodal sodium channel clusters remained unaffected.
  • Biochemical analysis showed decreased levels of myelin-associated glycoprotein, myelin basic protein, and NF155 in myelin.

Conclusions:

  • MAL plays a critical role in the maintenance of CNS paranodes.
  • MAL is essential for the proper trafficking and/or sorting of NF155 and other membrane proteins in oligodendrocytes.
  • Dysfunction of MAL leads to structural abnormalities and protein mislocalization in the myelin sheath.

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