Identification of paxillin domains interacting with β-catenin.
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.
Mesh Terms:
Adherens Junctions, Allosteric Site, Endothelial Cells, Escherichia coli, Focal Adhesions, Gene Expression Regulation, Glutathione Transferase, HEK293 Cells, Humans, Paxillin, Plasmids, Protein Binding, Protein Structure, Tertiary, Proto-Oncogene Proteins c-akt, Recombinant Proteins, Signal Transduction, beta Catenin
Adherens Junctions, Allosteric Site, Endothelial Cells, Escherichia coli, Focal Adhesions, Gene Expression Regulation, Glutathione Transferase, HEK293 Cells, Humans, Paxillin, Plasmids, Protein Binding, Protein Structure, Tertiary, Proto-Oncogene Proteins c-akt, Recombinant Proteins, Signal Transduction, beta Catenin
FEBS Lett.
Date: Jul. 30, 2012
PubMed ID: 22728435
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