Abstract
Coordination of actomyosin contraction and cell-cell junctions generates forces that can lead to tissue morphogenetic processes like the formation of neural tube (NT), however, its molecular mechanisms responsible for regulating and coupling this contractile network to cadherin adhesion remain to be fully elucidated. Here, using a gene trapping technology, we unveil the new player in this process, α-catulin, which shares sequence homology with vinculin and α-catenin. Ablation of α-catulin in mouse causes defective NT closure due to impairment of apical constriction, concomitant with apical actin and P-Mlc2 accumulation. Using a 3D culture model system, we showed that α-catulin localizes to the apical membrane and its removal alters the distribution of active RhoA and polarization. Actin cytoskeleton and P-Mlc2, downstream targets of RhoA, are not properly organized, with limited accumulation at the junctions, indicating a loss of junction stabilization. Our data suggest that α-catulin plays an important role during NT closure by acting as a scaffold for RhoA distribution, resulting in proper spatial activation of myosin to influence actin-myosin dynamics and tension at cell-cell adhesion.