In conclusion, our previous and the new data presented in this comment paper support the role of TPPP/p25 in the MT bundling in agreement with the title’s message of the Skoufias’s paper1 that focuses on the dimerization potency of this disordered, brain-specific MAP24. This issue does not seem to be affected by differences manifesting in the truncation sites: the Skoufias’s group chose shorter CORE segment based on bioinformatics analysis1 than we had published originally on the basis of multinuclear magnetic resonance study6. Based upon our previous and present in vitro and in vivo data obtained with the FL and truncated TPPP/p25 forms, we have established a molecular model for the maturation of the bundled MT structure stabilized by TPPP/p25 dimers (Fig. 4). We do not exclude other possible mechanisms such as the binding of the N- and C- termini to separate MTs. Nevertheless, the key issue is the crucial role of the unstructured termini, not in the dimerization but in the cross-linking of MTs, in which all segments (CORE, N- and C-termini) are involved with distinct binding affinity in a cooperative manner. The TPPP/p25-derived stabilization of the MT network seems to be of physiological importance in the development of projections in the course of the differentiation of oligodendrocytes17.