Direct interaction between selenoprotein P and tubulin.
Direct interaction between selenoprotein P and tubulin.
复制标题
硒蛋白 P 与微管蛋白之间的直接相互作用
DOI：
10.3390/ijms150610199
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发表时间：
2014-06-06
影响因子：
5.6
通讯作者：
Liu Q
中科院分区：
文献类型：
--
作者：
Du X;Qiu S;Wang Z;Wang R;Wang C;Tian J;Liu Q
硒是人体必需的微量元素，主要通过硒蛋白发挥其生物学功能。硒蛋白P （SelP）是人类已发现的25种硒蛋白中唯一含有多个硒半胱氨酸（Sec）的硒蛋白，被认为具有硒转运蛋白的功能。缺乏硒的小鼠会出现严重的神经功能障碍，并表现出广泛的脑干神经变性，这表明SelP在正常脑功能中起重要作用。为了进一步阐明SelP在大脑中的功能，利用酵母双杂交系统从人胎儿大脑cDNA文库中筛选SelP相互作用蛋白。我们的研究结果表明SelP与微管蛋白α 1a （TUBA1A）相互作用。通过荧光共振能量转移（FRET）和共免疫沉淀（co-IP）实验验证了SelP和微管蛋白之间的相互作用。我们进一步发现SelP通过其富含his的结构域与微管蛋白的c端相互作用，正如FRET和等温滴定量热法（ITC）测定所证明的那样。本文讨论了SelP和微管蛋白在大脑和阿尔茨海默病中相互作用的意义。
Selenium (Se), an essential trace element for human health, mainly exerts its biological function via selenoproteins. Among the 25 selenoproteins identified in human, selenoprotein P (SelP) is the only one that contains multiple selenocysteines (Sec) in the sequence, and has been suggested to function as a Se transporter. Upon feeding a selenium-deficient diet, mice lacking SelP develop severe neurological dysfunction and exhibit widespread brainstem neurodegeneration, indicating an important role of SelP in normal brain function. To further elucidate the function of SelP in the brain, SelP was screened by the yeast two-hybrid system from a human fetal brain cDNA library for interactive proteins. Our results demonstrated that SelP interacts with tubulin, alpha 1a (TUBA1A). The interaction between SelP and tubulin was verified by fluorescence resonance energy transfer (FRET) and co-immunoprecipitation (co-IP) assays. We further found that SelP interacts with the C-terminus of tubulin by its His-rich domain, as demonstrated by FRET and Isothermal Titration Calorimetry (ITC) assays. The implications of the interaction between SelP and tubulin in the brain and in Alzheimer’s disease are discussed.
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