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2016 ; 27
(18
): 2844-56
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Formin-mediated actin polymerization at cell-cell junctions stabilizes E-cadherin
and maintains monolayer integrity during wound repair
#MMPMID27440924
Rao MV
; Zaidel-Bar R
Mol Biol Cell
2016[Sep]; 27
(18
): 2844-56
PMID27440924
show ga
Cadherin-mediated cell-cell adhesion is required for epithelial tissue integrity
in homeostasis, during development, and in tissue repair. E-cadherin stability
depends on F-actin, but the mechanisms regulating actin polymerization at
cell-cell junctions remain poorly understood. Here we investigated a role for
formin-mediated actin polymerization at cell-cell junctions. We identify mDia1
and Fmnl3 as major factors enhancing actin polymerization and stabilizing
E-cadherin at epithelial junctions. Fmnl3 localizes to adherens junctions
downstream of Src and Cdc42 and its depletion leads to a reduction in F-actin and
E-cadherin at junctions and a weakening of cell-cell adhesion. Of importance,
Fmnl3 expression is up-regulated and junctional localization increases during
collective cell migration. Depletion of Fmnl3 or mDia1 in migrating monolayers
results in dissociation of leader cells and impaired wound repair. In summary,
our results show that formin activity at epithelial cell-cell junctions is
important for adhesion and the maintenance of epithelial cohesion during dynamic
processes, such as wound repair.