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首页> 美国卫生研究院文献>Molecular and Cellular Biology >Binding of Delta1 Jagged1 and Jagged2 to Notch2 Rapidly Induces Cleavage Nuclear Translocation and Hyperphosphorylation of Notch2
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Binding of Delta1 Jagged1 and Jagged2 to Notch2 Rapidly Induces Cleavage Nuclear Translocation and Hyperphosphorylation of Notch2

机译：Delta1Jagged1和Jagged2绑定到Notch2迅速诱导Notch2的分裂核易位和磷酸化。

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摘要

Delta1, Jagged1, and Jagged2, commonly designated Delta/Serrate/LAG-2 (DSL) proteins, are known to be ligands for Notch1. However, it has been less understood whether they are ligands for Notch receptors other than Notch1. Meanwhile, ligand-induced cleavage and nuclear translocation of the Notch protein are considered to be fundamental for Notch signaling, yet direct observation of the behavior of the Notch molecule after ligand binding, including cleavage and nuclear translocation, has been lacking. In this report, we investigated these issues for Notch2. All of the three DSL proteins bound to endogenous Notch2 on the surface of BaF3 cells, although characteristics of Jagged2 for binding to Notch2 apparently differed from that of Delta1 and Jagged1. After binding, the three DSL proteins induced cleavage of the membrane-spanning subunit of Notch2 (Notch2TM), which occurred within 15 min. In a simultaneous time course, the cleaved fragment of Notch2TM was translocated into the nucleus. Interestingly, the cleaved Notch2 fragment was hyperphosphorylated also in a time-dependent manner. Finally, binding of DSL proteins to Notch2 also activated the transcription of reporter genes driven by the RBP-Jκ-responsive promoter. Together, these data indicate that all of these DSL proteins function as ligands for Notch2. Moreover, the findings of rapid cleavage, nuclear translocation, and phosphorylation of Notch2 after ligand binding facilitate the understanding of the Notch signaling.
机译：众所周知，通常将Delta / Serrate / LAG-2（DSL）蛋白称为Delta1，Jagged1和Jagged2，它们是Notch1的配体。但是，人们对它们是否是Notch1以外的Notch受体的配体了解得很少。同时，Notch蛋白的配体诱导的裂解和核易位被认为是Notch信号转导的基础，但缺乏对配体结合后Notch分子行为的直接观察，包括裂解和核易位。在此报告中，我们调查了Notch2的这些问题。所有三种DSL蛋白都与BaF3细胞表面的内源性Notch2结合，尽管Jagged2与Notch2结合的特征显然不同于Delta1和Jagged1。结合后，这三种DSL蛋白诱导了Notch2的跨膜亚基（Notch2 TM ）的裂解，发生在15分钟内。在同时的时间过程中，Notch2 TM 的裂解片段被转移到细胞核中。有趣的是，切割的Notch2片段也以时间依赖性方式被过度磷酸化。最后，DSL蛋白与Notch2的结合也激活了RBP-Jκ反应启动子驱动的报告基因的转录。总之，这些数据表明所有这些DSL蛋白均充当Notch2的配体。此外，配体结合后Notch2的快速裂解，核易位和磷酸化的发现促进了对Notch信号传导的理解。

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