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Ena/VASP Proteins Can Regulate Distinct Modes of Actin Organization at Cadherin-adhesive ContactsD?V?

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Ena/VASP Proteins Can Regulate Distinct Modes of Actin Organization at Cadherin-adhesive ContactsD?V?
Id. 5313262
Idioma inglés
Titulo Ena/VASP Proteins Can Regulate Distinct Modes of Actin Organization at Cadherin-adhesive ContactsD?V?
Autor(es) Scott, Jeanie A.
Shewan, Annette M.
den Elzen, Nicole R.
Loureiro, Joseph J.
Gertler, Frank B.
Yap, Alpha S.
Localización http://www.pubmedcentral.gov/articlerender.fcgi?artid=1382300
Versión 1.0
Estado Final
Descripción 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.
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Copyright © 2006, The American Society for Cell Biology
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Fecha de contribución 01-dic-2006
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