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钙库操作性钙离子通道(store-operated calcium entry,SOCE)是介导胞外Ca2+进入细胞内的重要通道之一,其核心蛋白由位于内质网上的基质相互作用分子(stromal interaction molecule,STIM)和位于细胞膜上的Orai蛋白构成。目前研究发现,STIM蛋白存在STIM1和STIM2两种亚型,其主要功能略有不同。当内质网内钙库中Ca2+消耗之后,STIM蛋白通过其特殊的结构能够感受内质网内钙库中Ca2+浓度的变化,发生快速的转位和聚合化等激活反应,与质膜上的Orai蛋白偶联,实现SOCE通路的功能开放,引起Ca2+内流。当钙库中Ca2+得到补充之后,STIM蛋白与Orai蛋白缓慢解离即失活,通路关闭。目前对STIM蛋白结构的研究提示,通过其激活和失活机制不仅能够参与调节SOCE通路的开放与关闭,也参与对细胞内重要的细胞增殖、分化等功能活动调控。STIM蛋白可能成为治疗多种疾病的潜在的新靶点。
The store-operated calcium entry (SOCE) is one of the important channels that mediate the extracellular Ca2 + entry into the cell. Its core protein is composed of a stromal interaction molecule (STIM) located on the endoplasmic reticulum ) And Orai protein located on the cell membrane. The current study found that, STIM protein STIM1 and STIM2 exist two subtypes, its main function is slightly different. When Ca2 + in the endoplasmic reticulum is depleted, the STIM protein, through its special structure, can sense the change of Ca2 + concentration in the endoplasmic reticulum calcium stores, undergo rapid translocation and polymerization activation, Orai protein coupling, the function of SOCE pathway to open, causing Ca2 + influx. When Ca2 + in the calcium pool is replenished, the STIM protein is inactivated by slow dissociation of the Orai protein and the pathway is closed. The current research on the structure of STIM protein suggests that it can not only regulate the opening and closing of the SOCE pathway through its activation and inactivation mechanism, but also participate in the regulation of functional activities such as important cell proliferation and differentiation in the cell. STIM proteins may be potential new targets for the treatment of many diseases.