Format

Send to

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

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

Author information

1
Department of Cell and Developmental Biology, University of Illinois, Urbana-Champaign, IL 61801 USA.
2
Department of Cell and Developmental Biology, University of Illinois, Urbana-Champaign, IL 61801 USA vtang@illinois.edu.

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.

KEYWORDS:

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

PMID:
29748378
PMCID:
PMC6031380
[Available on 2019-06-15]
DOI:
10.1242/jcs.211334
Free full text

Supplemental Content

Full text links

Icon for HighWire
Loading ...
Support Center