The small myelin-associated glycoprotein binds to tubulin and microtubules

The myelin-associated glycoprotein (MAG) exists as two isoforms, differing only by their respective cytoplasmic domains, that have been suggested to function in the formation and maintenance of myelin. In the present study, a 50 kDa protein binding directly to the small MAG (S-MAG) cytoplasmic domai...

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Bibliographic Details
Published in:Brain research. Molecular brain research. 2001-02, Vol.87 (1), p.22-30
Main Authors: Kursula, Petri, Lehto, Veli-Pekka, Heape, Anthony M.
Format: Article
Language:English
Subjects:
Animals
Biological and medical sciences
Brain Neoplasms
Cell adhesion molecule
Fundamental and applied biological sciences. Psychology
Glioma
In Vitro Techniques
Isolated neuron and nerve. Neuroglia
Microtubule
Microtubules - metabolism
Molecular Sequence Data
Myelin
Myelin-associated glycoprotein
Myelin-Associated Glycoprotein - chemistry
Myelin-Associated Glycoprotein - genetics
Myelin-Associated Glycoprotein - metabolism
Nerve Fibers, Myelinated - metabolism
Protein Binding - physiology
Protein Folding
Protein Structure, Tertiary
Rats
Rats, Sprague-Dawley
Recombinant Proteins - chemistry
Recombinant Proteins - metabolism
Schwann cell
Schwann Cells - metabolism
Sciatic Nerve - metabolism
Sequence Homology, Amino Acid
Tubulin - metabolism
Tumor Cells, Cultured
Vertebrates: nervous system and sense organs
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Summary:The myelin-associated glycoprotein (MAG) exists as two isoforms, differing only by their respective cytoplasmic domains, that have been suggested to function in the formation and maintenance of myelin. In the present study, a 50 kDa protein binding directly to the small MAG (S-MAG) cytoplasmic domain was detected and identified as tubulin, the core component of the microtubular cytoskeleton. In vitro, the S-MAG cytoplasmic domain slowed the polymerization rate of tubulin and co-purified with assembled microtubules. A significant sequence homology was found between the tau family tubulin-binding repeats and the carboxy-terminus of S-MAG. Our results indicate that S-MAG is the first member of the Ig superfamily that can be classified as a microtubule-associated protein, and place S-MAG in a dynamic structural complex that could participate in linking the axonal surface and the myelinating Schwann cell cytoskeleton.
ISSN:0169-328X
1872-6941
DOI:10.1016/S0169-328X(00)00270-9