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JNK regulates binding of α‐catenin to adherens junctions and cell‐cell adhesion

We recently reported that c‐Jun N‐termi‐nal kinase (JNK) is associated with adherens junctions and phosphorylates β‐catenin at serine 33/37 and threonine 41. Here, we report that inhibition of JNK led to formation of adherens junctions, which was accompanied by dissociation of α‐catenin from the β‐catenin/ E‐cadherin complex and increased association of α‐catenin with the cytoskeleton. Conversely, activation of JNK increased binding of α‐catenin to β‐catenin, which was blocked by the JNK inhibitor SP600125 or JNK siRNA. In addition, inhibition of JNK failed to lead to adherens junction formation in cells where α‐catenin was absent or knocked down. Conversely, introduction of α‐catenin restored the responsiveness of cells to JNK inhibition and led to cell‐cell adhesion. Experiments with domain deletion mutants showed that binding of α‐catenin to β‐catenin was required for transport of adherens junction complexes to the cell surface, while binding to actin was required for translocation to the cell‐cell contact sites. Collectively, our results suggest that JNK affects the association of α‐cate‐nin with the adherens junction complex and regulates adherens junctions.—Lee, M.‐H., Padmashali, R., Koria, P., Andreadis, S. T. JNK regulates binding of α‐catenin to adherens junctions and cell‐cell adhesion. FASEB J. 25, 613–623 (2011). www.fasebj.org