Atomic force microscopy (AFM) imaging suggests that stromal interaction molecule 1 (STIM1) binds to Orai1 with sixfold symmetry
Atomic force microscopy (AFM) imaging suggests that stromal interaction molecule 1 (STIM1) binds to Orai1 with sixfold symmetry
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DOI：
10.1016/j.febslet.2014.06.054
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发表时间：
2014-08-25
期刊：
影响因子：
3.5
通讯作者：
Edwardson, J. Michael
中科院分区：
文献类型：
--
作者：
Balasuriya, Dilshan;Srivats, Shyam;Edwardson, J. Michael
从内质网（ER）管腔Ca2+的消耗触发Ca2+释放激活的Ca2+ (CRAC)通道在质膜的开放。CRAC通道由基质相互作用分子1 （STIM1）激活，STIM1是一种内质网蛋白，可感知Ca2+存储耗尽并与通道的孔隙形成亚基Orai1相互作用。CRAC通道的亚单位化学计量学存在争议。在这里，我们提供了证据，使用原子力显微镜（AFM）成像，Orai1组装为六聚体，并且STIM1以六倍对称性结合Orai1。STIM1以单体、二聚体和多聚体串状结构的形式与Orai1结合，形成Orai1六聚体之间的连接。我们的研究结果为STIM1和Orai1之间相互作用的本质提供了新的见解。蛋白质相互作用的结构化总结：Orai1通过抗标签共免疫沉淀与STIM1物理相互作用（View相互作用）Orai1和STIM1通过原子力显微镜结合（View相互作用）STIM1和STIM1通过荧光显微镜共定位（View相互作用）STIM1和STIM1通过原子力显微镜结合（1,2）Orai1和Orai1通过原子力显微镜结合（View相互作用）(C) 2014 Federation of European Biochemical Societies。Elsevier B.V.版权所有。
Depletion of Ca2+ from the endoplasmic reticulum (ER) lumen triggers the opening of Ca2+ release-activated Ca2+ (CRAC) channels at the plasma membrane. CRAC channels are activated by stromal interaction molecule 1 (STIM1), an ER resident protein that senses Ca2+ store depletion and interacts with Orai1, the pore-forming subunit of the channel. The subunit stoichiometry of the CRAC channel is controversial. Here we provide evidence, using atomic force microscopy (AFM) imaging, that Orai1 assembles as a hexamer, and that STIM1 binds to Orai1 with sixfold symmetry. STIM1 associates with Orai1 in the form of monomers, dimers, and multimeric string-like structures that form links between the Orai1 hexamers. Our results provide new insights into the nature of the interactions between STIM1 and Orai1.Structured summary of protein interactions:Orai1 physically interacts with STIM1 by anti tag coimmunoprecipitation (View interaction)Orai1 and STIM1 bind by atomic force microscopy (View interaction)STIM1 and Orai1 colocalize by fluorescence microscopy (View interaction)STIM1 and STIM1 bind by atomic force microscopy (1, 2)Orai1 and Orai1 bind by atomic force microscopy (View interaction) (C) 2014 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.