Ameloblastoma (AB) is the most common benign epithelial odontogenic tumor 
occurring in the jawbone. AB is a slowly growing tumor but sometimes shows a 
locally invasive and an aggressive growth pattern with a marked bone resorption. 
In addition, the local recurrence and distant metastasis of AB also sometimes 
occurs, which resembles one of the typical malignant potentials. From these 
points of view, to understand better the mechanisms of AB cell migration or 
invasion is necessary for the better clinical therapy and improvements of the 
patients' quality of life. Microtubules in eukaryotic cells reveal the shape of 
hollow cylinders made up of polymerized alpha (α)- and beta (β)-tubulin dimers 
and form the cytoskeleton together with microfilaments and intermediate 
filaments. Microtubules play important roles in cell migration by undergoing 
assembly and disassembly with post-translational modifications. Stability of 
microtubules caused by their acetylation is involved in cell migration. In this 
study, we investigated the expression and distribution of acetylated α-tubulin 
and alpha-tubulin N-acetyltransferase 1 (αTAT1), an enzyme which acetylates 
Lys-40 in α-tubulin, in AB specimens, and analyzed how tubulin was acetylated by 
αTAT1 activation in a human AB cell line, AM-1. Finally, we clarified that 
TGF-β-activated kinase1 (TAK1) was phosphorylated by TGF-β stimulation, then, 
induced tubulin acetylation via αTAT1 activation, which subsequently activated 
the migration and invasion of AB cells.