Figure 9.

Schematic representation of the greater impact of Tau phosphorylation on mitochondrial transport compared to nonphosphorylated Tau. A, Tau is a space-making protein attached to the MT surface. When Tau is not phosphorylated at Ser199/Ser202/Thr205, the N-terminal domain is folded. This conformation does not produce much resistance force against mitochondrial movement because MTs are in relatively close proximity. B, Tau phosphorylation at Ser199/Ser202/Thr205 may extend the projection domain away from the MT surface, increasing the repulsive forces between MTs. In this conformation, mitochondria encounter greater MT resistance to the slowing or arresting of their movement.