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首页> 外文期刊>Proceedings of the National Academy of Sciences of the United States of America >Notch interferes with the scaffold function of JNK-interacting protein 1 to inhibit the JNK signaling pathway
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Notch interferes with the scaffold function of JNK-interacting protein 1 to inhibit the JNK signaling pathway

机译：Notch干扰JNK相互作用蛋白1的支架功能以抑制JNK信号通路

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摘要

The transmembrane protein Notch is cleaved by gamma-secretase to yield an active form, Notch intracellular domain (Notch-IC), in response to the binding of ligands, such as Jagged. Notch-IC contributes to the regulation of a variety of cellular events, including cell fate determination during embryonic development as well as cell growth, differentiation, and survival. We now show that Notch1-IC suppresses the scaffold activity of c-Jun N-terminal kinase (JNK)-interacting protein 1 (JIP1) in the JNK signaling pathway. Notch1-IC physically associated with the JNK binding domain of JlP1 and thereby interfered with the interaction between JlP1 and JNK. JlP1 mediated the activation of JNK1 induced by glucose deprivation in mouse embryonic fibroblasts, and ectopic expression of Notch1-IC inhibited JNK activation and apoptosis triggered by glucose deprivation. Taken together, these findings suggest that Notch1-IC negatively regulates the JNK pathway by disrupting the scaffold function of JIP1.
机译：响应于配体的结合，例如锯齿状，跨膜蛋白Notch被γ-分泌酶切割以产生活性形式Notch细胞内结构域（Notch-IC）。 Notch-IC有助于调节各种细胞事件，包括确定胚胎发育过程中的细胞命运以及细胞生长，分化和存活。现在，我们显示Notch1-IC抑制JNK信号通路中c-Jun N末端激酶（JNK）相互作用蛋白1（JIP1）的支架活性。 Notch1-IC与JlP1的JNK结合域物理相关，从而干扰JlP1与JNK之间的相互作用。 JlP1介导了小鼠胚胎成纤维细胞中葡萄糖剥夺诱导的JNK1活化，Notch1-IC的异位表达抑制了葡萄糖剥夺引发的JNK活化和凋亡。综上所述，这些发现表明Notch1-IC通过破坏JIP1的支架功能而负调控JNK通路。

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