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Developmental partitioning of myelin basic protein into membrane microdomains

L S DeBruin1, J D Haines, L A Wellhauser

  • 1Department of Molecular and Cellular Biology and Biophysics Interdepartmental Group, University of Guelph, Guelph, Ontario, Canada.

Journal of Neuroscience Research
|March 18, 2005
PubMed

Insights

Myelin basic protein (MBP) and its modifications localize to specific membrane microdomains, with developmental changes observed in lipid raft composition. This suggests novel roles for MBP beyond myelin compaction.

Area of Science:

  • Neuroscience
  • Cell Biology
  • Biochemistry

Background:

  • Myelin basic protein (MBP) is crucial for myelin sheath integrity.
  • Posttranslational modifications of MBP suggest potential roles in signal transduction.
  • Myelin contains specific membrane microdomains, including lipid rafts, that are not fully characterized.

Purpose of the Study:

  • To investigate the spatial and temporal distribution of MBP and its modified forms within myelin membrane microdomains.
  • To characterize the composition of lipid rafts in developing and mature bovine myelin.

Main Methods:

  • Extraction of myelin membranes using Brij 96V, CHAPS, and Triton X-100 detergents.
  • Isolation of detergent-resistant membranes (DRMs) representing lipid rafts via sucrose density gradient centrifugation.
  • Cholesterol depletion using methyl-beta-cyclodextrin to disrupt myelin rafts.
  • Analysis of protein localization in DRMs and non-raft fractions.
  • Colocalization studies in cultured mouse oligodendrocytes.

Main Results:

  • Myelin rafts were identified and characterized, and their disruption by cholesterol depletion was confirmed.
  • Phospho-Thr97-MBP was enriched in DRMs of mature myelin using CHAPS detergent.
  • Citrullinated and methylated MBP were found in non-raft microdomains.
  • Golli-MBP, Fyn, Lyn, and CNP were enriched in DRMs of early myelin.
  • Oligodendrocyte cultures supported the colocalization of raft components.

Conclusions:

  • There is a developmental regulation of posttranslationally modified MBP forms into specific membrane microdomains.
  • These findings suggest that MBP may have functions beyond myelin compaction, potentially involving signal transduction within distinct membrane domains.

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