Lipid phosphate phosphatase 3 stabilization of beta-catenin induces endothelial cell migration and formation of branching point structures.
Endothelial cell (EC) migration, cell-cell adhesion, and the formation of branching point structures are considered hallmarks of angiogenesis; however, the underlying mechanisms of these processes are not well understood. Lipid phosphate phosphatase 3 (LPP3) is a recently described p120-catenin-associated integrin ligand localized in adherens junctions (AJs) of ECs. Here, we ... tested the hypothesis that LPP3 stimulates beta-catenin/lymphoid enhancer binding factor 1 (beta-catenin/LEF-1) to induce EC migration and formation of branching point structures. In subconfluent ECs, LPP3 induced expression of fibronectin via beta-catenin/LEF-1 signaling in a phosphatase and tensin homologue (PTEN)-dependent manner. In confluent ECs, depletion of p120-catenin restored LPP3-mediated beta-catenin/LEF-1 signaling. Depletion of LPP3 resulted in destabilization of beta-catenin, which in turn reduced fibronectin synthesis and deposition, which resulted in inhibition of EC migration. Accordingly, reexpression of beta-catenin but not p120-catenin in LPP3-depleted ECs restored de novo synthesis of fibronectin, which mediated EC migration and formation of branching point structures. In confluent ECs, however, a fraction of p120-catenin associated and colocalized with LPP3 at the plasma membrane, via the C-terminal cytoplasmic domain, thereby limiting the ability of LPP3 to stimulate beta-catenin/LEF-1 signaling. Thus, our study identified a key role for LPP3 in orchestrating PTEN-mediated beta-catenin/LEF-1 signaling in EC migration, cell-cell adhesion, and formation of branching point structures.
Mesh Terms:
Amino Acid Sequence, Animals, Catenins, Cell Adhesion, Cell Line, Cell Movement, Endothelial Cells, Fibronectins, Humans, Isoenzymes, Lymphoid Enhancer-Binding Factor 1, Molecular Sequence Data, Neovascularization, Physiologic, PTEN Phosphohydrolase, Phosphatidate Phosphatase, RNA Interference, Signal Transduction, beta Catenin
Amino Acid Sequence, Animals, Catenins, Cell Adhesion, Cell Line, Cell Movement, Endothelial Cells, Fibronectins, Humans, Isoenzymes, Lymphoid Enhancer-Binding Factor 1, Molecular Sequence Data, Neovascularization, Physiologic, PTEN Phosphohydrolase, Phosphatidate Phosphatase, RNA Interference, Signal Transduction, beta Catenin
Mol. Cell. Biol.
Date: Apr. 01, 2010
PubMed ID: 20123964
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