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首页> 外文期刊>Proceedings of the National Academy of Sciences of the United States of America >Each rhodopsin molecule binds its own arrestin
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Each rhodopsin molecule binds its own arrestin

机译：每个视紫红质分子结合其自身的抑制蛋白

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摘要

Arrestins (Arrs) are ubiquitous regulators of the most numerous family of signaling proteins, G protein-coupled receptors. Two models of the Arr-receptor interaction have been proposed: the binding of one Arr to an individual receptor or to two receptors in a dimer. To determine the binding stoichiometry in vivo, we used rod photore-ceptors where rhodopsin (Rh) and Arr are expressed at comparably high levels and where Arr localization in the light is determined by its binding to activated Rh. Genetic manipulation of the expression of both proteins shows that the maximum amount of Arr that moves to the Rh-containing compartment exceeds 80%, but not 100%, of the molar amount of Rh present. In vitro experiments with purified proteins confirm that Arr "saturates" Rh at a 1:1 ratio. Thus, a single Rh molecule is necessary and sufficient to bind Arr. Remarkable structural conservation among receptors and Arrs strongly suggests that all Arr subtypes bind individual molecules of their cognate receptors.
机译：Arrestins（Arrs）是信号蛋白家族中最多的调节因子，G蛋白偶联受体。已经提出了Arr-受体相互作用的两种模型：一种Arr与一个单独的受体或二聚体中的两个受体的结合。为了确定体内结合化学计量，我们使用了棒状光感受器，其中视紫红质（Rh）和Arr的表达水平较高，而Arr在光中的定位则取决于其与活化Rh的结合。两种蛋白质表达的遗传操作表明，移动到含Rh的区室的最大Arr量超过所存在Rh摩尔量的80％，但不是100％。纯化蛋白的体外实验证实Arr以1：1的比例“饱和”了Rh。因此，单个Rh分子是必要且足以结合Arr的。受体和Arrs之间的显着结构保守性强烈表明，所有Arr亚型均与其同源受体的单个分子结合。

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