Dynamic recruitment of axin by Dishevelled protein assemblies
Dynamic recruitment of axin by Dishevelled protein assemblies
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DOI：
10.1242/jcs.002956
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发表时间：
2007-07-15
影响因子：
4
通讯作者：
Bienz, Mariann
中科院分区：
文献类型：
--
作者：
Schwarz-Romond, Thomas;Metcalfe, Ciara;Bienz, Mariann
Dishevelled（Dvl）蛋白是Wnt信号通路的细胞质组分，其控制动物发育期间的许多细胞命运决定。在Wnt信号传导期间，Dvl结合卷曲跨膜受体的细胞内结构域，并且还结合轴蛋白以阻断其活性，这导致β-连环蛋白的激活，并因此导致转录开关。我们先前已经报道了哺乳动物Dvl 2的DIX结构域允许其形成动态蛋白质组装体。在这里，我们表明，这些Dvl 2组件招募轴，也酪蛋白激酶I β。使用GFP标记的Dvl 2和轴蛋白的光漂白实验来研究它们相互作用的动力学，我们发现Dvl 2组装体对轴蛋白- GFP的募集伴随着轴蛋白-GFP的动力学性质的显著加速。我们还表明，Dvl 2和轴蛋白之间的相互作用保持高度动态，即使在Wnt诱导的重新定位到质膜。我们讨论了如何招募酪蛋白激酶I的Dvl 2组件可能会影响招聘轴的质膜在Wnt信号。
Dishevelled (Dvl) proteins are cytoplasmic components of the Wnt signalling pathway, which controls numerous cell fate decisions during animal development. During Wnt signalling, Dvl binds to the intracellular domain of the frizzled transmembrane receptors, and also to axin to block its activity, which results in the activation of beta-catenin and, consequently, in a transcriptional switch. We have previously reported that the DIX domain of mammalian Dvl2 allows it to form dynamic protein assemblies. Here, we show that these Dvl2 assemblies recruit axin, and also casein kinase I epsilon. Using photobleaching experiments of GFP- tagged Dvl2 and axin to study the dynamics of their interaction, we found that the recruitment of axin- GFP by Dvl2 assemblies is accompanied by a striking acceleration of the dynamic properties of axin-GFP. We also show that the interaction between Dvl2 and axin remains highly dynamic even after Wnt- induced relocation to the plasma membrane. We discuss how the recruitment of casein kinase I epsilon by Dvl2 assemblies might impact on the recruitment of axin to the plasma membrane during Wnt signalling.