Scratching the surface: native mass spectrometry of peripheral membrane protein complexes.

Scratching the surface: native mass spectrometry of peripheral membrane protein complexes.
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浅谈:外周膜蛋白复合物的天然质谱分析。

DOI:
10.1042/bst20190787
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发表时间:
2020
影响因子:
3.9
通讯作者:
Landreh,Michael
Landreh,Michael
中科院分区:
生物学3区
文献类型:
--
作者:
Sahin,Cagla;Reid,DesereeJ;Marty,MichaelT;Landreh,Michael

文献摘要

相似文献

越来越多的整体膜蛋白已被证明通过选择性地与特定脂质相互作用来调节其活性。通过脂质相互作用调节生物功能的能力扩展到仅与脂质双分子层外周相关的多种蛋白质组。然而,由于这些相互作用的短暂性和混杂性,其结构基础仍然具有挑战性。近年来,天然质谱法作为一种研究膜蛋白中脂质相互作用的新工具受到人们的关注。在这里,我们概述了如何将针对整体膜蛋白开发的天然质谱策略应用于外周膜蛋白的结构和功能。具体来说,天然质谱研究蛋白质与洗涤剂溶解的脂质复合物、与脂质纳米盘结合以及从天然类脂质囊泡中释放,这些研究都为脂质相互作用的作用提供了新的视角。天然质谱捕获和询问蛋白质-蛋白质、蛋白质-配体和蛋白质-脂质相互作用的独特能力为外周膜蛋白生物学的研究开辟了令人兴奋的新途径。
A growing number of integral membrane proteins have been shown to tune their activity by selectively interacting with specific lipids. The ability to regulate biological functions via lipid interactions extends to the diverse group of proteins that associate only peripherally with the lipid bilayer. However, the structural basis of these interactions remains challenging to study due to their transient and promiscuous nature. Recently, native mass spectrometry has come into focus as a new tool to investigate lipid interactions in membrane proteins. Here, we outline how the native MS strategies developed for integral membrane proteins can be applied to generate insights into the structure and function of peripheral membrane proteins. Specifically, native MS studies of proteins in complex with detergent-solubilized lipids, bound to lipid nanodiscs, and released from native-like lipid vesicles all shed new light on the role of lipid interactions. The unique ability of native MS to capture and interrogate protein–protein, protein–ligand, and protein–lipid interactions opens exciting new avenues for the study of peripheral membrane protein biology.