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JNK phosphorylates β-catenin and regulates adherens junctions

Meng-Horng Lee^*,1, Piyush Koria^*,1, Jun Qu^, and Stelios T. Andreadis^*,,2

^* Bioengineering Laboratory, Department of Chemical and Biological Engineering,

Department of Pharmaceutical Sciences; and

Center for Excellence in Bioinformatics and Life Sciences, University at Buffalo, The State University of New York, Amherst, New York, USA

² Correspondence: Bioengineering Laboratory, 908 Furnas Hall, Department of Chemical and Biological Engineering, University at Buffalo, State University of New York, Amherst, NY 14260, USA. E-mail: sandread{at}buffalo.edu

The c-Jun amino-terminal kinase (JNK) is an important player in inflammation, proliferation, and apoptosis. More recently, JNK was found to regulate cell migration by phosphorylating paxillin. Here, we report a novel role of JNK in cell adhesion. Specifically, we provide evidence that JNK binds to E-cadherin/β-catenin complex and phosphorylates β-catenin at serine 37 and threonine 41, the sites also phosphorylated by GSK-3β. Inhibition of JNK kinase activity using dominant-negative constructs reduces phosphorylation of β-catenin and promotes localization of E-cadherin/β-catenin complex to cell-cell contact sites. Conversely, activation of JNK induces β-catenin phosphorylation and disruption of cell contacts, which are prevented by JNK siRNA. We propose that JNK binds to β-catenin and regulates formation of adherens junctions, ultimately controlling cell-to-cell adhesion.—Lee, M.-H., Koria, P., Qu, J., Andreadis, S. T. JNK phosphorylates β-catenin and regulates adherens junctions.

Key Words: cell adhesion • E-cadherin • epithelial development • cell invasion • SP600125 • okadaic acid