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10.1083/jcb.201406135

http://scihub22266oqcxt.onion/10.1083/jcb.201406135
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suck abstract from ncbi


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pmid25452388
      J+Cell+Biol 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.
  • |*Cell Adhesion [MESH]
  • |Actin Cytoskeleton/*metabolism [MESH]
  • |Animals [MESH]
  • |Cadherins/*metabolism [MESH]
  • |Cytoskeletal Proteins/genetics/*metabolism [MESH]
  • |Dogs [MESH]
  • |Gene Knockdown Techniques [MESH]
  • |Madin Darby Canine Kidney Cells [MESH]
  • |Microscopy, Fluorescence [MESH]
  • |Protein Transport [MESH]
  • |rac GTP-Binding Proteins/genetics/*metabolism [MESH]


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