Ena/VASP proteins can regulate distinct modes of actin organization at cadherin-adhesive contacts

Scott, Jeanie A., Shewan, Annette M., den Elzen, Nicole R., Loureiro, Joseph J., Gertler, Frank B. and Yap, Alpha S. (2006) Ena/VASP proteins can regulate distinct modes of actin organization at cadherin-adhesive contacts. Molecular Biology of The Cell, 17 3: 1085-1095. doi:10.1191/mbc.E05-07-0644

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Author Scott, Jeanie A.
Shewan, Annette M.
den Elzen, Nicole R.
Loureiro, Joseph J.
Gertler, Frank B.
Yap, Alpha S.
Title Ena/VASP proteins can regulate distinct modes of actin organization at cadherin-adhesive contacts
Journal name Molecular Biology of The Cell   Check publisher's open access policy
ISSN 1059-1524
Publication date 2006
Sub-type Article (original research)
DOI 10.1191/mbc.E05-07-0644
Open Access Status File (Publisher version)
Volume 17
Issue 3
Start page 1085
End page 1095
Total pages 11
Editor Sandra L. Schmid
Place of publication Bethesda
Publisher The American Society for Cell Biology
Collection year 2006
Language eng
Subject C1
270105 Cellular Interactions (incl. Adhesion, Matrix, Cell Wall)
780105 Biological sciences
Abstract Functional interactions between classical cadherins and the actin cytoskeleton involve diverse actin activities, including filament nucleation, cross-linking, and bundling. In this report, we explored the capacity of Ena/VASP proteins to regulate the actin cytoskeleton at cadherin-adhesive contacts. We extended the observation that Ena/vasodilator-stimulated phosphoprotein (VASP) proteins localize at cell-cell contacts to demonstrate that E-cadherin homophilic ligation is sufficient to recruit Mena to adhesion sites. Ena/VASP activity was necessary both for F-actin accumulation and assembly at cell-cell contacts. Moreover, we identified two distinct pools of Mena within individual homophilic adhesions that cells made when they adhered to cadherin-coated substrata. These Mena pools localized with Arp2/3-driven cellular protrusions as well as at the tips of cadherin-based actin bundles. Importantly, Ena/VASP activity was necessary for both modes of actin activity to be expressed. Moreover, selective depletion of Ena/VASP proteins from the tips of cadherin-based bundles perturbed the bundles without affecting the protrusive F-actin pool. We propose that Ena/VASP proteins may serve as higher order regulators of the cytoskeleton at cadherin contacts through their ability to modulate distinct modes of actin organization at those contacts.
Keyword Cadherin-adhesive Contacts
Ena/vasp Proteins
Cell Biology
Cell-cell Adhesion
Adherens Junctions
Fibroblast Motility
Arp2/3 Complex
Q-Index Code C1

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Created: Wed, 15 Aug 2007, 08:42:35 EST