Arrestins: ubiquitous regulators of cellular signaling pathways.
Arrestins: ubiquitous regulators of cellular signaling pathways.
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DOI：
10.1186/gb-2006-7-9-236
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发表时间：
2006
期刊：
影响因子：
12.3
通讯作者：
Gurevich VV
中科院分区：
文献类型：
--
作者：
Gurevich EV;Gurevich VV
阻滞素是一个小的蛋白质家族，调节G蛋白偶联受体的信号传递和运输，也是细胞质和细胞核中普遍存在的信号调节因子。在脊椎动物中，阻滞素是一个由四种蛋白质组成的家族，调节着数百种不同的G蛋白偶联受体(GPCRs)的信号和运输。在昆虫、原脊索动物和线虫中也发现了arrestin同源物。真菌和原生生物有相关的蛋白质，但没有真正的拦阻蛋白。结构信息只适用于自由(未结合)的脊椎动物拦阻蛋白，并表明保守的整体折叠是拉长的，由两个结构域组成，每个结构域的核心由一个七链β-三明治组成。两个主要的分子内相互作用使两个结构域保持正确的相对方向，但在受体结合的过程中，这两个相互作用都不稳定，这表明结合的arrestin的构象有很大的不同。除了与数百种gpr亚型结合外，拦阻蛋白还与其他类别的膜受体和20多种令人惊讶的不同类型的可溶性信号蛋白相互作用。因此，阻滞素在细胞质和细胞核中起着普遍存在的信号调节作用。
The arrestins are a small family of proteins that regulate the signaling and trafficking of G-protein-coupled receptors and also serve as ubiquitous signaling regulators in the cytoplasm and nucleus. In vertebrates, the arrestins are a family of four proteins that regulate the signaling and trafficking of hundreds of different G-protein-coupled receptors (GPCRs). Arrestin homologs are also found in insects, protochordates and nematodes. Fungi and protists have related proteins but do not have true arrestins. Structural information is available only for free (unbound) vertebrate arrestins, and shows that the conserved overall fold is elongated and composed of two domains, with the core of each domain consisting of a seven-stranded β-sandwich. Two main intramolecular interactions keep the two domains in the correct relative orientation, but both of these interactions are destabilized in the process of receptor binding, suggesting that the conformation of bound arrestin is quite different. As well as binding to hundreds of GPCR subtypes, arrestins interact with other classes of membrane receptors and more than 20 surprisingly diverse types of soluble signaling protein. Arrestins thus serve as ubiquitous signaling regulators in the cytoplasm and nucleus.
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影响因子：
64.8
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