Subcellular fractionation and association with the cytoskeleton of messengers encoding myelin proteins

The targeting of polypeptides to restricted cytoplasmic domains by means of mRNA sorting is a widespread phenomena utilized by many cell types. In the central nervous system, in situ hybridization analysis has shown previously that the mRNAs encoding several myelin-specific proteins are specifically located within the myelinating processes of oligodendrocytes. Here, by means of biochemical and subcellular fractionation methods, we show that a myelin fraction is selectively enriched in those mRNAs. The four major myelin basic protein (MBP) mRNAs that arise by alternative splicing of exons II and VI of the MBP gene are concentrated in this subcellular fraction. Furthermore, an interaction of MBP and MOBP 81A mRNAs with the cytoskeleton was observed. This interaction might serve to mediate the anchoring of these messengers after translocation to the subcellular site of translation.