Cadherin-directed actin assembly: E-cadherin physically associates with the Arp2/3 complex to direct actin assembly in nascent adhesive contacts

Kovacs, Eva M., Goodwin, Marita K., Ali, Radiya G., Paterson, Andrew D. and Yap, Alpha S. (2002) Cadherin-directed actin assembly: E-cadherin physically associates with the Arp2/3 complex to direct actin assembly in nascent adhesive contacts. Current Biology, 12 5: 379-382. doi:10.1016/S0960-9822(02)00661-9


Author Kovacs, Eva M.
Goodwin, Marita K.
Ali, Radiya G.
Paterson, Andrew D.
Yap, Alpha S.
Title Cadherin-directed actin assembly: E-cadherin physically associates with the Arp2/3 complex to direct actin assembly in nascent adhesive contacts
Journal name Current Biology   Check publisher's open access policy
ISSN 0960-9822
Publication date 2002-03-05
Sub-type Article (original research)
DOI 10.1016/S0960-9822(02)00661-9
Volume 12
Issue 5
Start page 379
End page 382
Total pages 4
Place of publication Cambridge
Publisher Cell Press
Language eng
Subject C1
270105 Cellular Interactions (incl. Adhesion, Matrix, Cell Wall)
780105 Biological sciences
Abstract Cadherin cell adhesion molecules are major determinants of tissue patterning which function in cooperation with the actin cytoskeleton [1-4]. In the context of stable adhesion [1], cadherin/catenin complexes are often envisaged to passively scaffold onto cortical actin filaments. However, cadherins also form dynamic adhesive contacts during wound healing and morphogenesis [2]. Here actin polymerization has been proposed to drive cell surfaces together [5], although F-actin reorganization also occurs as cell contacts mature [6]. The interaction between cadherins and actin is therefore likely to depend on the functional state of adhesion. We sought to analyze the relationship between cadherin homophilic binding and cytoskeletal activity during early cadherin adhesive contacts. Dissecting the specific effect of cadherin ligation alone on actin regulation is difficult in native cell-cell contacts, due to the range of juxtacrine signals that can arise when two cell surfaces adhere [7]. We therefore activated homophilic ligation using a specific functional recombinant protein. We report the first evidence that E-cadherin associates with the Arp2/3 complex actin nucleator and demonstrate that cadherin binding can exert an active, instructive influence on cells to mark sites for actin assembly at the cell surface.
Keyword Biochemistry & Molecular Biology
Cell-cell Adhesion
Small Gtpase Rac
Polymerization
Morphogenesis
Q-Index Code C1
Additional Notes DOI: 10.1016/S0960-9822(02)00661-9

Document type: Journal Article
Sub-type: Article (original research)
Collections: Excellence in Research Australia (ERA) - Collection
Institute for Molecular Bioscience - Publications
 
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Created: Wed, 15 Aug 2007, 04:57:02 EST