JNK phosphorylates β-catenin and regulates adherens junctions
JNK phosphorylates β-catenin and regulates adherens junctions
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DOI：
10.1096/fj.08-117804
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发表时间：
2009-11-01
期刊：
影响因子：
4.8
通讯作者：
Andreadis, Stelios T.
中科院分区：
文献类型：
--
作者：
Lee, Meng-Horng;Koria, Piyush;Andreadis, Stelios T.
c-Jun氨基末端激酶（JNK）是炎症、增殖和凋亡中的重要参与者。最近，JNK被发现通过磷酸化桩蛋白来调节细胞迁移。在这里，我们报告了JNK在细胞粘附中的新作用。具体来说，我们提供的证据表明，JNK结合E-钙粘蛋白/β-连环蛋白复合物和磷酸化β-连环蛋白的丝氨酸37和苏氨酸41，该网站也磷酸化GSK-3 β。使用显性负性构建体抑制JNK激酶活性减少β-连环蛋白的磷酸化并促进E-钙粘蛋白/β-连环蛋白复合物定位于细胞-细胞接触位点。相反，JNK的活化诱导β-连环蛋白磷酸化和细胞接触的破坏，这被JNK siRNA阻止。我们认为JNK与β-连环蛋白结合并调节粘附连接的形成，最终控制细胞与细胞的粘附。李，M.- H、Koria，P.，Qu，J.，Andreadis，S. T. JNK磷酸化β-连环蛋白并调节粘附连接。FASEB J.23，3874-3883（2009）. www.fasebj.org
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/beta-catenin complex and phosphorylates beta-catenin at serine 37 and threonine 41, the sites also phosphorylated by GSK-3 beta. Inhibition of JNK kinase activity using dominant-negative constructs reduces phosphorylation of beta-catenin and promotes localization of E-cadherin/beta-catenin complex to cell-cell contact sites. Conversely, activation of JNK induces beta-catenin phosphorylation and disruption of cell contacts, which are prevented by JNK siRNA. We propose that JNK binds to beta-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 beta-catenin and regulates adherens junctions. FASEB J. 23, 3874-3883 (2009). www.fasebj.org