Abstract
Willin is a FERM-domain protein, which is related to the Drosophila Expanded, a protein known to be a component of the Hippo signaling pathway. We recently showed that Willin localizes at the apical junctional complex (AJC) in epithelial cells together with Par3 and regulates the contractility of the circumferential actomyosin cables by recruiting aPKC to the AJC. However, it remains unresolved how Willin becomes associated with the AJC. Here, we report that Willin binds to nectins, Ig-family proteins, which also localize at the AJC via their homophilic or heterophilic interactions, and this binding participates in the junctional recruitment of Willin. In addition, we report that the positioning of nectins at the AJC is dependent on their binding to afadin. Thus, our results suggest that the nectin-afadin interaction plays a role in the correct localization of Willin.
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