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

Journal of Cell Science
Nivetha Kannan, Vivian W Tang

Abstract

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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Citations

Dec 25, 2019·Proceedings of the National Academy of Sciences of the United States of America·John Xiao He LiWilliam M Brieher
Nov 15, 2019·The Journal of Cell Biology·Yuou Wang, William M Brieher
Jul 31, 2020·Current Opinion in Physiology·Susana Lechuga, Andrei I Ivanov
Jun 9, 2021·Proceedings of the National Academy of Sciences of the United States of America·John Xiao He LiWilliam M Brieher
Oct 28, 2021·The Journal of Cell Biology·Aurélie MangonAli Badache

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