Recently in Scientific Reports, Skoufias and co-workers published a paper entitled “Self protein-protein interactions are involved in TPPP/p25 mediated microtubule bundling” in which a number of data are presented on the interaction of Tubulin Polymerization Promoting Protein (TPPP/p25) forms with tubulin and microtubule (MT)1. In our previous studies following the discovery of TPPP/p25 as a microtubule associated protein (MAP) our data support a model for TPPP/p25-induced MT bundling2345. Our reported findings in relation to the structure and function of TPPP/p25 - relevant to the Skoufias’s paper1 - are as follows: i) it is a disordered protein with unstructured N- and C-termini straddling a flexible CORE region as detected by multinuclear magnetic resonance spectroscopy6; ii) its dimers display higher tubulin assembly activity than the monomers4; ii) it induces MT assembly coupled with bundling activity resulting in resistance against anti-MT agents7. These findings indirectly support a mechanism for the stabilization of the MT network by dimeric TPPP/p25.