The structure of the C-terminal domain of the protein kinase AtSOS2 bound to the calcium sensor AtSOS3
The structure of the C-terminal domain of the protein kinase AtSOS2 bound to the calcium sensor AtSOS3
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DOI：
10.1016/j.molcel.2007.04.013
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发表时间：
2007-05-11
期刊：
影响因子：
16
通讯作者：
Albert, Armando
中科院分区：
文献类型：
--
作者：
Sanchez-Barrena, Maria Jose;Fujii, Hiroaki;Albert, Armando
植物SOS2家族的蛋白激酶及其相互作用的激活剂SOS3家族的钙结合蛋白，共同作用于解码不同环境刺激引起的钙信号。SOS2被Ca-SOS3激活，随后使离子转运体SOS1磷酸化，从而在盐胁迫下实现细胞内离子的动态平衡。SOS2蛋白激酶家族的成员除了具有激酶活性外，还可以与蛋白磷酸酶2Cs结合。Ca-SOS3与SOS2的C端调节部分的二元络合物的晶体结构解决了关于SOS2作为激酶和磷酸酶结合蛋白的双重功能的核心问题。通过与未结合的SOS3结构的比较，揭示了该蛋白家族及其相互作用的钙感受器的分子功能基础。此外，我们的研究表明，SOS2的磷酸酶相互作用结构域的结构定义了一个从酵母到人类保守的支架模块。
The plant SOS2 family of protein kinases and their interacting activators, the SOS3 family of calcium-binding proteins, function together in decoding calcium signals elicited by different environmental stimuli. SOS2 is activated by Ca-SOS3 and subsequently phosphorylates the ion transporter SOS1 to bring about cellular ion homeostasis under salt stress. In addition to possessing the kinase activity, members of the SOS2 family of protein kinases can bind to protein phosphatase 2Cs. The crystal structure of the binary complex of Ca-SOS3 with the C-terminal regulatory moiety of SOS2 resolves central questions regarding the dual function of SOS2 as a kinase and a phosphatase-binding protein. A comparison with the structure of unbound SOS3 reveals the basis of the molecular function of this family of kinases and their interacting calcium sensors. Furthermore, our study suggests that the structure of the phosphatase-interaction domain of SOS2 defines a scaffold module conserved from yeast to human.