Schematic representation of the model. (A) Summary of the results. The binding of KIF5C to β-tubulin will push this subunit to rotate around the T7 loop, leading to the elongation of the axial pitch (top, blue and black arrows). The lattice structure of the microtubule will restrict the conformation and the arrangement of tubulin subunits so that the conformational changes of the microtubule will take place in a cooperative manner (bottom). The conformational changes of the microtubule will be recognized by the interaction between kinesin’s L11-α4 junction and the H3′ helix of α-tubulin (top, green arrow). (B) A hypothetical model of the propagation of the conformational changes by the processive run of a kinesin dimer. A single protofilament of microtubule is shown with a kinesin dimer (a pair of green balls). The nucleotide states are shown in each head (ø, nucleotide-free; D, ADP; T, ATP). Bluish color shows the tubulin subunits in GDP conformation. Red to purple color shows the strain of the conformational changes propagating from the bound nucleotide-free head. (C) A model for the stochastic oscillation of kinesin accumulation in juvenile neuron. A gray Y-shaped neuron with three neurites is shown with GDP- and GTP-like conformation microtubules in blue and red, respectively. Green small circles represent kinesin molecules. See the main text for details.