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2014 ; 207
(5
): 577-87
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An Elmo-Dock complex locally controls Rho GTPases and actin remodeling during
cadherin-mediated adhesion
#MMPMID25452388
Toret CP
; Collins C
; Nelson WJ
J Cell Biol
2014[Dec]; 207
(5
): 577-87
PMID25452388
show ga
Cell-cell contact formation is a dynamic process requiring the coordination of
cadherin-based cell-cell adhesion and integrin-based cell migration. A
genome-wide RNA interference screen for proteins required specifically for
cadherin-dependent cell-cell adhesion identified an Elmo-Dock complex. This was
unexpected as Elmo-Dock complexes act downstream of integrin signaling as Rac
guanine-nucleotide exchange factors. In this paper, we show that Elmo2 recruits
Dock1 to initial cell-cell contacts in Madin-Darby canine kidney cells. At
cell-cell contacts, both Elmo2 and Dock1 are essential for the rapid recruitment
and spreading of E-cadherin, actin reorganization, localized Rac and Rho GTPase
activities, and the development of strong cell-cell adhesion. Upon completion of
cell-cell adhesion, Elmo2 and Dock1 no longer localize to cell-cell contacts and
are not required subsequently for the maintenance of cell-cell adhesion. These
studies show that Elmo-Dock complexes are involved in both integrin- and
cadherin-based adhesions, which may help to coordinate the transition of cells
from migration to strong cell-cell adhesion.