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首页> 外文期刊>Biophysical Chemistry: An International Journal Devoted to the Physical Chemistry of Biological Phenomena >P130Cas substrate domain is intrinsically disordered as characterized by single-molecule force measurements
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P130Cas substrate domain is intrinsically disordered as characterized by single-molecule force measurements

机译：P130Cas底物结构域本质上是无序的，通过单分子力测量来表征

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摘要

P130Cas is a docking protein essentially coordinating tyrosine-kinase-based signaling pathways associated with cell adhesion and migration etc. Its central substrate domain (CasSD) can bind to Crk and includes 15 YxxP motifs, where most tyrosine phosphorylation happens. It has been shown that CasSD can be stretched to promote phosphorylation, the mechanism of which needs to be explored in detail. Thus, it is important to uncover the native structure(s) of CasSD and the structural changes associated with mechanical stretching, both of which are still unclear. Here, we used atomic force microscopy force mode and magnetic tweezers to stretch individual molecules of CasSD constructs. Our results showed that the CasSD domain was intrinsically disordered. Natively, CasSD domains took many conformations beside random coils, while most of these conformations possessed limited mechanical stability. In magnetic tweezers experiments, the intramolecular interactions stabilizing the varied native conformations of CasSD were found similar in strength. Such diversity in native conformations of CasSD domains, as discovered here, should play important role in their signaling functions and their limited strength should be relevant to the mechanical activation of those signaling pathways.
机译：P130Cas是一种对接蛋白，主要用于协调与细胞粘附和迁移等相关的基于酪氨酸激酶的信号传导途径。它的中央底物结构域（CasSD）可以与Crk结合，并包含15个YxxP基序，其中大多数酪氨酸磷酸化发生。已经显示CasSD可以被拉伸以促进磷酸化，其机理需要详细探讨。因此，重要的是要揭示CasSD的一个或多个天然结构以及与机械拉伸相关的结构变化，这两者仍不清楚。在这里，我们使用原子力显微镜力模式和磁性镊子拉伸CasSD构建体的单个分子。我们的结果表明，CasSD域本质上是无序的。本机地，CasSD域除了随机线圈外还具有许多构象，而这些构象中的大多数具有有限的机械稳定性。在磁性镊子实验中，发现稳定CasSD各种天然构象的分子内相互作用强度相似。此处发现的CasSD域天然构象的这种多样性应在其信号传导功能中发挥重要作用，其有限的强度应与那些信号通路的机械活化有关。

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