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Intracellular movement of p120‐catenin in endothelial cells and implications for transcriptional regulation

In endothelium, the adherens junction‐associated protein p120‐catenin (p120ctn) is known for cell‐cell adhesion, but a role in transcriptional regulation is unclear. We postulate that the junctional pool of p120ctn may redistribute to regulate transcription under conditions of loss of organized junctions. At subconfluent growth, immunofluorescent dectection of p120ctn in endothelial cells (EC) shows distribution primarily in the nucleus as confirmed with DAPI stain colocalization. In contrast, in fully confluent monolayers, p120ctn localizes at the plasma membrane with barely detectable expression in either cytoplasm or nucleus. The disruption of EC junctions with TNF (100 U/ml for 1 hr) causes a marked shift of p120ctn from the membrane to the nuclear and perinuclear regions. We observe that the EC express Kaiso, a transcription factor reported to be a binding partner with p120ctn. Transfection of minimal promoter reporter plasmid containing Kaiso binding elements (pKBS‐Luc) results in 30% repression of luciferase activity in EC. Finally, we show that siRNA‐mediated knockdown of p120ctn increased 2‐fold the KBS reporter activity, suggesting that p120ctn‐Kaiso represses gene transcription. Together, these data implicate p120ctn as a key player in regulating transcription in endothelial cells. The study is supported by NIH HL093715.