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

Nivetha Kannan, Vivian Tang

Research output: Contribution to journalArticle

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.

Original languageEnglish (US)
JournalJournal of cell science
Volume131
Issue number12
DOIs
StatePublished - Jun 27 2018

Fingerprint

Actinin
Intercellular Junctions
Cadherins
Myosins
Epithelial Cells
Cell Adhesion
Actomyosin
Membranes
Actin Cytoskeleton
Actins

Keywords

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

ASJC Scopus subject areas

  • Cell Biology

Cite this

Myosin-1c promotes E-cadherin tension and force-dependent recruitment of α-actinin to the epithelial cell junction. / Kannan, Nivetha; Tang, Vivian.

In: Journal of cell science, Vol. 131, No. 12, 27.06.2018.

Research output: Contribution to journalArticle

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