Arp2/3 activity is necessary for efficient formation of E-cadherin adhesive contacts

Verma, S., Shewan, A. M., Scott, J. A., Helwani, F. M., den Elzen, N. R., Miki, H., Takenawa, T. and Yap, A. S. (2004) Arp2/3 activity is necessary for efficient formation of E-cadherin adhesive contacts. Journal of Biological Chemistry, 279 32: 34062-34070. doi:10.1074/jbc.M404814200

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Author Verma, S.
Shewan, A. M.
Scott, J. A.
Helwani, F. M.
den Elzen, N. R.
Miki, H.
Takenawa, T.
Yap, A. S.
Title Arp2/3 activity is necessary for efficient formation of E-cadherin adhesive contacts
Journal name Journal of Biological Chemistry   Check publisher's open access policy
ISSN 0021-9258
Publication date 2004-01-01
Sub-type Article (original research)
DOI 10.1074/jbc.M404814200
Open Access Status File (Publisher version)
Volume 279
Issue 32
Start page 34062
End page 34070
Total pages 9
Place of publication Bethesda, U.S.
Publisher American Society for Biochemistry and Molecular Biology, Inc.
Collection year 2004
Language eng
Subject C1
270105 Cellular Interactions (incl. Adhesion, Matrix, Cell Wall)
780105 Biological sciences
0601 Biochemistry and Cell Biology
Abstract Classical cadherin adhesion molecules are fundamental determinants of cell-cell recognition that function in cooperation with the actin cytoskeleton. Productive cadherin-based cell recognition is characterized by a distinct morphological process of contact zone extension, where limited initial points of adhesion are progressively expanded into broad zones of contact. We recently demonstrated that E-cadherin ligation recruits the Arp2/3 actin nucleator complex to the plasma membrane in regions where cell contacts are undergoing protrusion and extension. This suggested that Arp2/3 might generate the protrusive forces necessary for cell surfaces to extend upon one another during contact assembly. We tested this hypothesis in mammalian cells by exogenously expressing the CA region of N-WASP. This fragment, which potently inhibits Arp2/3-mediated actin assembly in vitro, also effectively reduced actin assembly at cadherin adhesive contacts. Blocking Arp2/3 activity by this strategy profoundly reduced the ability of cells to extend cadherin adhesive contacts but did not affect cell adhesiveness. These findings demonstrate that Arp2/3 activity is necessary for cells to efficiently extend and assemble cadherin-based adhesive contacts.
Keyword Biochemistry & Molecular Biology
Cell-cell Adhesion
Phosphatidylinositol 3-kinase
Actin Nucleation
Binding-activity
Plasma-membrane
Complex
Dynamics
Polymerization
Morphogenesis
Mechanisms
Q-Index Code C1

 
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Created: Wed, 15 Aug 2007, 14:51:01 EST