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First published online 1 August 2006
doi: 10.1242/jcs.03027

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Regulation of epithelial wound closure and intercellular adhesion by interaction of AF6 with actin cytoskeleton

Institute of Medical Virology, University of Zurich, Gloriastrasse 30, CH-8006 Zurich, Switzerland

^* Author for correspondence (e-mail: moelling{at}immv.unizh.ch)

Accepted 28 April 2006

AF6 is a human multi-domain protein involved in signaling and organization of cell junctions during embryogenesis. Its homologue in rat is called afadin. Three different AF6 transcripts are known, but only isoform 1 (AF6i1) has been characterized as protein. We focused on the AF6 isoform 3 (AF6i3), which differs from the AF6i1 by an additional C-terminal F-actin-binding site. Knockdown of AF6i3 in epithelial cells, which express only this isoform, resulted in impaired E-cadherin-dependent intercellular adhesion due to concomitantly reduced association of E-cadherin with F-actin and p120-catenin. Impaired intercellular adhesion also accelerated wound closure due to increased directionality of cell migration and delayed de novo formation of cell junctions. In contrast to AF6i3, the AF6i1 displayed a reduced association with the actin cytoskeleton and did not stabilize intercellular adhesion. Therefore, we propose that the AF6i3 protein stabilizes E-cadherin-dependent adhesion during dynamic processes, such as wound closure and formation of cell junctions, by linking the E-cadherin-catenin complex to the actin cytoskeleton via its F-actin-binding site.

Key words: AF6 isoform 3, F-actin-binding site, E-cadherin, Cell-cell adhesion, Collective cell migration, Directionality

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