Department of Cell and Molecular Biology, John A. Burns School of Medicine, University of Hawaii, Honolulu, HI, USA.
Department of Cell and Molecular Biology, John A. Burns School of Medicine, University of Hawaii, Honolulu, HI, USA.
Cell Calcium. 2018 Mar;70:76-86. doi: 10.1016/j.ceca.2017.05.001. Epub 2017 May 4.
The human selenoprotein family contains 25 members that share the common feature of containing the amino acid, selenocysteine (Sec). Seven selenoproteins are localized to the endoplasmic reticulum (ER) and exhibit different structural features contributing to a range of cellular functions. Some of these functions are either directly or indirectly related to calcium (Ca) flux or homeostasis. The presence of the unique Sec residue within these proteins allows some to exert oxidoreductase activity, while the function of the Sec in other ER selenoproteins remains unclear. Some functional insight has been achieved by identifying domains within the ER selenoproteins or through the identification of binding partners. For example, selenoproteins K and N (SELENOK AND SELENON) have been characterized through interactions detected with the inositol 1,4,5-triphosphate receptors (IP3Rs) and the SERCA2b pump, respectively. Others have been linked to chaperone functions related to ER stress or Ca homeostasis. This review summarizes the details gathered to date regarding the ER-resident selenoproteins and their effect on Ca regulated pathways and outcomes in cells.
人类硒蛋白家族包含 25 个成员，它们都具有一个共同的特征，即含有氨基酸硒代半胱氨酸 (Sec)。7 种硒蛋白定位于内质网 (ER)，具有不同的结构特征，有助于多种细胞功能。其中一些功能直接或间接地与钙 (Ca) 流或动态平衡有关。这些蛋白质中独特的 Sec 残基的存在使一些具有氧化还原酶活性，而 Sec 在其他 ER 硒蛋白中的功能仍不清楚。通过鉴定 ER 硒蛋白中的结构域或通过鉴定结合伴侣，已经获得了一些功能上的认识。例如，通过与肌醇 1,4,5-三磷酸受体 (IP3Rs) 和 SERCA2b 泵的相互作用，已经对硒蛋白 K 和 N (SELENOK 和 SELENON) 进行了表征。其他的则与 ER 应激或 Ca 动态平衡相关的伴侣功能有关。本文综述了迄今为止关于 ER 内定位的硒蛋白及其对 Ca 调节途径和细胞中结果的影响的详细信息。
