The cell adhesion molecule TMIGD1 binds to moesin and regulates tubulin acetylation and cell migration

Abstract Background The cell adhesion molecule transmembrane and immunoglobulin (Ig) domain containing1 (TMIGD1) is a novel tumor suppressor that plays important roles in regulating cell–cell adhesion, proliferation cycle. However, the mechanisms of TMIGD1 signaling are not yet fully elucidated. Results binds to ERM family proteins moesin ezrin, an evolutionarily conserved RRKK motif on carboxyl terminus mediates interaction with N-terminal domains ezrin. governs apical localization as loss mice altered ezrin epithelial cells. In culture, inhibited moesin-induced filopodia-like protrusions migration. More importantly, stimulated Lysine (K40) acetylation ?-tubulin promoted mitotic spindle organization CRISPR/Cas9-mediated knockout impaired TMIGD1-mediated filamentous (F)-actin organization. Conclusions regulates their cellular localization. Moesin critical TMIGD1-dependent ?-tubulin, Our findings offer molecular framework for understanding complex functional interplay between regulation assembly, have wide-ranging implications physiological pathological processes such cancer progression.