Native mass spectrometry reveals the simultaneous binding of lipids and zinc to rhodopsin
Native mass spectrometry reveals the simultaneous binding of lipids and zinc to rhodopsin
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DOI：
10.1016/j.ijms.2020.116477
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发表时间：
2021-02-01
影响因子：
1.8
通讯作者：
Marty, Michael T.
中科院分区：
文献类型：
--
作者：
Norris, Carolanne E.;Keener, James E.;Marty, Michael T.
视紫红质是一种典型的G蛋白偶联受体，负责低光水平下的视觉。虽然视紫红质的光活化级联反应是很好的理解，它仍然不清楚如何结合到受体的脂质和锌耦合。使用本机质谱，我们开发了一种新的数据分析策略去卷积锌和脂质结合的视紫红质的蛋白形式，并研究了脂质和锌结合之间的变构相互作用。我们发现，磷脂酰胆碱结合视紫红质具有更大的亲和力比磷脂酰丝氨酸或磷脂酰乙醇胺，并结合所有脂质锌的影响，但具有不同的效果。相反，锌结合相对不受脂质干扰。总体而言，这些数据表明，脂质结合可以强烈和不同的金属离子的影响。(C)2020爱思唯尔B.V.保留所有权利。
Rhodopsin, a prototypical G-protein-coupled receptor, is responsible for scoptic vision at low-light levels. Although rhodopsin's photoactivation cascade is well understood, it remains unclear how lipid and zinc binding to the receptor are coupled. Using native mass spectrometry, we developed a novel data analysis strategy to deconvolve zinc and lipid bound to the proteoforms of rhodopsin and investigated the allosteric interaction between lipids and zinc binding. We discovered that phosphatidylcholine bound to rhodopsin with a greater affinity than phosphatidylserine or phosphatidylethanolamine, and that binding of all lipids was influenced by zinc but with different effects. In contrast, zinc binding was relatively unperturbed by lipids. Overall, these data reveal that lipid binding can be strongly and differentially influenced by metal ions. (C) 2020 Elsevier B.V. All rights reserved.