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首页> 外文期刊>Proceedings of the National Academy of Sciences of the United States of America >β-Arrestin1 modulates lymphoid enhancer factor transcriptional activity through interaction with phosphorylated dishevelled proteins
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β-Arrestin1 modulates lymphoid enhancer factor transcriptional activity through interaction with phosphorylated dishevelled proteins

机译:β-Arrestin1通过与磷酸化的斑驳蛋白相互作用来调节淋巴增强因子转录活性

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摘要

One aspect of the function of the β-arrestins is to serve as scaffold or adapter molecules coupling G-protein coupled receptors (GPCRs) to signal transduction pathways distinct from traditional second messenger pathways. Here we report the identification of Dishev- elled 1 and Dishevelled 2 (Dvl1 and Dvl2) as β-arrestin1 (βarr1) interacting proteins. Dvl proteins participate as key intermediates in signal transmission from the seven membrane-spanning Frizzled receptors leading to inhibition of glycogen synthase kinase-3β (GSK-3β), stabilization of β-catenin, and activation of the lymphoid enhancer factor (LEF) transcription factor.
机译:β-arrestin功能的一方面是用作将G蛋白偶联受体(GPCR)偶联至不同于传统第二信使途径的信号转导途径的支架或衔接子分子。在这里,我们报告鉴定Dishevelled 1和Disheveled 2(Dvl1和Dvl2)为β-arrestin1(βarr1)相互作用蛋白。 Dvl蛋白作为关键中间体参与来自七个跨膜卷曲蛋白受体的信号传递,从而导致糖原合酶激酶-3β(GSK-3β)的抑制,β-catenin的稳定和淋巴增强因子(LEF)转录因子的激活。

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