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Updated: Aug 10, 2026

Quantitative Microtubule Fractionation Technique to Separate Stable Microtubules, Labile Microtubules, and Free Tubulin in Mouse Tissues
Published on: November 17, 2023
The small myelin-associated glycoprotein binds to tubulin and microtubules
P Kursula1, V P Lehto, A M Heape
1Department of Pathology, University of Oulu, P.O. Box 5000, FIN-90014, Oulu, Finland. petri.kursula@oulu.fi
Abstract:
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.
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