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The Department of Molecular Biology and Biochemistry, Osaka University Graduate School of Medicine/Faculty of Medicine, Suita, Osaka 565-0871, Japan

In epithelial cells, tight junctions (TJs) and adherens junctions (AJs) form junctional complexes. At AJs, cadherins and nectins are the major cell-cell adhesion molecules. Nectins first form cell–cell adhesions and then recruit cadherins to the nectin-based cell–cell adhesion sites to form AJs in coordination with the activation of integrin _vß₃, followed by the formation of TJs. We previously demonstrated that when MDCK cells precultured at a low Ca²⁺ concentration were treated with the protein kinase C (PKC) activator 12-O-tetradecanoyl-phorbol-13-acetate (TPA), incomplete AJs and a TJ-like structure were achieved. However, it remains unknown how PKC is activated and how it regulates the formation of cell–cell junctions. When MDCK cells precultured at a low Ca²⁺ concentration were treated with TPA, incomplete AJs were formed without the activation of integrin _vß₃. Treatment of cells with TPA also enhanced the phosphorylation of FAK, which transmits the outside-in signal of integrin and plays a role in the nectin-induced formation of AJs. In addition, inhibition of PKC suppressed the formation of AJs. These results indicate that the activation of PKC functions downstream of integrin _vß₃ and upstream of FAK, and is important for the nectin-induced formation of AJs.

^* Correspondence: E-mail: ytakai{at}molbio.med.osaka-u.ac.jp

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