Myosin-1c promotes E-cadherin tension and force-dependent recruitment of α-actinin to the epithelial cell junction

J Cell Sci. 2018 Jun 27;131(12):jcs211334. doi: 10.1242/jcs.211334.


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.

Keywords: Cell–cell adhesion; Junction; Mechanobiology; Myosin; Synaptopodin; α-actinin.

Publication types

  • Research Support, N.I.H., Extramural

MeSH terms

  • Actinin / metabolism*
  • Cadherins / metabolism*
  • Epithelial Cells / metabolism*
  • Humans
  • Intercellular Junctions / metabolism*
  • Myosin Type II / metabolism*


  • Cadherins
  • Actinin
  • Myosin Type II