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首页> 外文期刊>Journal of Molecular Biology >A Novel Polar Core and Weakly Fixed C-Tail in Squid Arrestin Provide New Insight into Interaction with Rhodopsin
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A Novel Polar Core and Weakly Fixed C-Tail in Squid Arrestin Provide New Insight into Interaction with Rhodopsin

机译：鱿鱼逮捕中的一种新颖的极性核心和弱固定的C尾，提供了与罗地脂相互作用的新洞察力

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摘要

Photoreceptors of the squidLoligo pealeicontain a G-protein-coupled receptor (GPCR) signaling system that activates phospholipase C in response to light. Analogous to the mammalian visual system, signaling of the photoactivated GPCR rhodopsin is terminated by binding of squid arrestin (sArr). sArr forms a light-dependent, high-affinity complex with squid rhodopsin, which does not require prior receptor phosphorylation for interaction. This is at odds with classical mammalian GPCR desensitization where an agonist-bound phosphorylated receptor is needed to break stabilizing constraints within arrestins, the so-called “three-element interaction” and “polar core” network, before a stable receptor–arrestin complex can be established. Biophysical and mass spectrometric analysis of the squid rhodopsin–arrestin complex indicates that in contrast to mammalian arrestins, the sArr C-tail is not involved in a stable three-element interaction. We determined the crystal structure of C-terminally truncated sArr that adopts a basal conformation common to arrestins and is stabilized by a series of weak but novel polar core interactions. Unlike mammalian arrestin-1, deletion of the sArr C-tail does not influence kinetic properties of complex formation of sArr with the receptor. Hydrogen–deuterium exchange studies revealed the footprint of the light-activated rhodopsin on sArr. Furthermore, double electron–electron resonance spectroscopy experiments provide evidence that receptor-bound sArr adopts a conformation different from the one known for arrestin-1 and molecular dynamics simulations reveal the residues that account for the weak three-element interaction. Insights gleaned from studying this system add to our general understanding of GPCR–arrestin interaction.
机译：Squidloligo泡孔的光感受器A响应于光而激活磷脂酶C的G蛋白偶联受体（GPCR）信号传导系统。类似于哺乳动物视觉系统，通过鱿鱼诱导（SARR）的结合终止了光活化的GPCR roOdopsin的信号传导。 SARR形成具有鱿鱼罗霉蛋白的光依赖性高亲和力络合物，其不需要以前的受体磷酸化进行相互作用。这与典型哺乳动物GPCR脱敏的差异，其中需要在稳定的受体 - 抑制综合体之前破坏捕获素内的激动剂的磷酸化受体，以在稳定的受体 - 逮捕型复合物之前建立。鱿鱼罗经蛋白酶 - 抑制复合物的生物物理和质谱分析表明与哺乳动物捕获素相比，SARR C尾部不涉及稳定的三元相互作用。我们确定了C末端截断SAR的晶体结构，其采用ARRIVERINS共同的基础构象，并通过一系列弱但新的极性核心相互作用稳定。与哺乳动物虫害不同，SARR C-TAIN的缺失不会影响与受体的复杂形成复杂形成的动力学性质。氢氘交换研究揭示了SARR上的光活性杂色蛋白酶的足迹。此外，双电子 - 电子共振光谱实验提供了据证明受体结合的SARR采用与诱导-1的已知不同的构象，分子动力学模拟揭示了用于弱三元相互作用的残留物。从研究该系统中收集的洞察力在于我们对GPCR-Alctionin互动的一般理解。

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