Abstract
Barrier-protective agonists induce association of focal adhesions (FA) and adherens junctions (AJ) in endothelial cells. Here we identified specific domains of FA protein paxillin interacting with AJ protein and examined regulation of paxillin domain interactions with β-catenin by Rac GTPase. Co-expression of paxillin LD-1,2; LD-3,4; LIM-1,2; and LIM-3,4 domains with β-catenin showed exclusive interaction of LIM-1,2 and LIM-3,4 with β-catenin, which was enhanced by agonist-induced Rac activation or expression of activated Rac mutant. These results demonstrate a novel function of paxillin LIM domains in targeting β-catenin in a Rac-dependent manner, which may play a role in Rac-dependent control of FA-AJ interactions and monolayer integrity.Structured summary of protein interactions:Paxillin binds to Beta-catenin by pull down (View interaction)Beta-catenin physically interacts with Paxillin by anti bait coimmunoprecipitation (View interaction)Paxillin physically interacts with GIT2 by pull down (View interaction)Paxillin physically interacts with Beta-catenin by pull down (View Interaction: 1, 2)
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