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 language | English (US) |
|---|---|
| Journal | Journal of cell science |
| Volume | 131 |
| Issue number | 12 |
| DOIs | |
| State | Published - Jun 27 2018 |
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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 journal › Article
}
TY - JOUR
T1 - Myosin-1c promotes E-cadherin tension and force-dependent recruitment of α-actinin to the epithelial cell junction
AU - Kannan, Nivetha
AU - Tang, Vivian
PY - 2018/6/27
Y1 - 2018/6/27
N2 - 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.
AB - 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.
KW - Cell–cell adhesion
KW - Junction
KW - Mechanobiology
KW - Myosin
KW - Synaptopodin
KW - α-actinin
UR - http://www.scopus.com/inward/record.url?scp=85068186446&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=85068186446&partnerID=8YFLogxK
U2 - 10.1242/jcs.211334
DO - 10.1242/jcs.211334
M3 - Article
C2 - 29748378
AN - SCOPUS:85068186446
VL - 131
JO - Journal of Cell Science
JF - Journal of Cell Science
SN - 0021-9533
IS - 12
ER -