Investigation via ion pore transplantation of the putative relationship between glutamate receptors and K+ channels
Investigation via ion pore transplantation of the putative relationship between glutamate receptors and K+ channels
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DOI：
10.1016/j.mcn.2006.08.004
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发表时间：
2006-12-01
影响因子：
3.5
通讯作者：
Hollmann, Michael
中科院分区：
文献类型：
--
作者：
Hoffmann, Jutta;Villmann, Carmen;Hollmann, Michael
离子型谷氨酸受体(IGluRs)和钾通道(K+通道)的孔域在结构上有几个相似之处。为了测试功能兼容性，我们将原核生物、无脊椎动物和脊椎动物K+通道的孔区转移到具有药理代表性的iGluRs中，反之亦然。尽管嵌合蛋白在细胞表面表达，但在45个孔嵌合体中只有一个具有离子通道功能：海人藻酸受体亚单位GluR6，它携带原核生物谷氨酸类K+选择性GluR0的孔环和相邻的跨膜结构域，在孔移植时继承了供体孔的几种电生理特性。这表明，尽管iGluR和K+通道孔在结构上相似，但缺乏功能兼容性，因此K+通道孔不能被iGluR门控机制门控，反之亦然。然而，K+选择性孔可以在iGluR序列环境中被门控，给定类似于GluR0中似乎存在的信号转导机制。(C)2006 Elsevier Inc.保留所有权利。
The pore domains of ionotropic glutamate receptors (iGluRs) and potassium channels (K+ channels) show several structural similarities. To test for functional compatibility, we transferred pore regions from prokaryotic, invertebrate, and vertebrate K+ channels into pharmacologically representative iGluRs and vice versa. Although the chimeric proteins were expressed on the cell surface, only one of 45 pore chimeras showed ion channel function: The kainate receptor subunit GluR6, carrying the pore loop plus adjacent transmembrane domains of the prokaryotic, glutamategated, K+-selective GluR0, adopted several electrophysiological properties of the donor pore upon pore transplantation. This suggests that, despite structural similarities between iGluR and K+ channel pores, there is a lack of functional compatibility so that K+ channel pores cannot be gated by the iGluR gating machinery, and vice versa. However, K+-selective pores can be gated in an iGluR sequence environment, given a similar signal transduction mechanism as appears to be present in GluR0. (c) 2006 Elsevier Inc. All rights reserved.