A novel tension-sensitive junctional protein, synaptopodin, can relay biophysical input from cellular actomyosin contractility to induce biochemical changes at cell–cell contacts, resulting in structural reorganization of the junctional complex and epithelial barrier maturation.

Actomyosin II contractility in epithelial cell plays an essential role in tension-dependent adhesion strengthening. One key unsettling question is how cellular contraction transmits force to the nascent cell-cell adhesion when there is no stable attachment between the nascent adhesion complex and actin filament. Here, we show that myosin-1c is localized to the lateral membrane of polarized epithelial cells and facilitates the coupling between actin and cell-cell adhesion. Knockdown of myosin-1c compromised the integrity of the lateral membrane, reduced the generation of tension at E-cadherin, decreased the strength of cell-cell cohesion in an epithelial cell monolayer and prevented force-dependent recruitment of junctional α-actinin. Application of exogenous force to cell-cell adhesions in a myosin-1c-knockdown cell monolayer fully rescued the localization defect of α-actinin, indicating that junction mechanoregulation remains intact in myosin-1c-depleted cells. Our study identifies a role of myosin-1c in force transmission at the lateral cell-cell interface and underscores a non-junctional contribution to tension-dependent junction regulation.

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