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Myelin-associated oligodendrocytic basic protein mRNAs reside at different subcellular locations
R M Gould1, C M Freund, E Barbarese
1Department of Pharmacology, New York State Institute for Basic Research in Developmental Disabilities, Staten Island, New York 10314-6330, USA.
Journal of Neurochemistry
|October 28, 1999
Summary
Myelin-associated oligodendrocytic basic protein (MOBP) mRNA localization differs based on alternative splicing. Specific MOBP mRNAs are found at myelin assembly sites, while others remain in the oligodendrocyte cell body.
Area of Science:
- Neuroscience
- Molecular Biology
- Cell Biology
Background:
- Myelin basic protein (MBP) and myelin-associated oligodendrocytic basic protein (MOBP) are crucial myelin proteins.
- MBP mRNA is known to localize to sites of myelin sheath assembly in oligodendrocytes.
Purpose of the Study:
- To investigate the subcellular localization of various MOBP mRNA variants.
- To determine if MOBP mRNA localization is influenced by alternative splicing.
Main Methods:
- Subcellular fractionation of oligodendrocytes.
- Analysis of mRNA distribution within different cellular compartments.
Main Results:
- Four MOBP mRNA variants (MOBP-71, MOBP-81A, MOBP-99, MOBP-169) were enriched in myelin fractions.
- These myelin-associated MOBP mRNAs share a common exon (exon 8b) with sequence similarity to the MBP mRNA RNA transport sequence (RTS).
- Three other MOBP mRNA variants (MOBP-69, MOBP-81B, MOBP-170) lacking exon 8b were primarily found in the oligodendrocyte soma.
Conclusions:
- Alternative splicing significantly influences MOBP mRNA distribution within oligodendrocytes.
- The presence of exon 8b, similar to MBP mRNA RTS, likely directs specific MOBP mRNAs to myelin assembly sites.