Probing Membrane Protein Interactions and Signaling Molecule Homeostasis in Plants by Förster Resonance Energy Transfer Analysis.
Probing Membrane Protein Interactions and Signaling Molecule Homeostasis in Plants by Förster Resonance Energy Transfer Analysis.
复制标题
通过福斯特共振能量转移分析探测植物中的膜蛋白相互作用和信号分子稳态。
DOI：
10.1093/jxb/erab445
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发表时间：
2021-10
影响因子：
6.9
通讯作者：
Jingjing Xing
中科院分区：
文献类型：
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作者：
Zhikun Duan;Kaiwen Li;Wenwen Duan;Junli Zhang;Jingjing Xing
膜蛋白在信号转导、转运和代谢中起着关键作用。因此，破译膜蛋白之间的相互作用为信号转导和蛋白质复合体的时空组织提供了至关重要的信息。然而，检测膜蛋白在其天然环境中的相互作用和行为仍然是困难的。Förster共振能量转移(FRET)是一种在不破坏膜蛋白局部环境的情况下量化膜蛋白动态相互作用和组装的有力工具，提供了纳米尺度的空间信息和纳秒尺度的时间信息。本文简要介绍了FRET的基本原理，并对用于分析植物膜蛋白的FRET新技术(如FRET、HOMO-FRET和smFRET)的发展现状进行了评价。我们还描述了各种基于FRET的生物传感器，用于量化信号分子的动态平衡和激酶的激活状态。此外，我们总结了这些先进的FRET传感器在探测膜蛋白相互作用、化学计量学和蛋白质聚集方面的最新应用，这些应用揭示了活植物细胞中膜蛋白的复杂生物学功能。
Membrane proteins have key functions in signal transduction, transport, and metabolism. Therefore, deciphering the interactions between membrane proteins provides crucial information on signal transduction and the spatiotemporal organization of protein complexes. However, detecting the interactions and behaviors of membrane proteins in their native environments remains difficult. Förster resonance energy transfer (FRET) is a powerful tool for quantifying the dynamic interactions and assembly of membrane proteins without disrupting their local environment, supplying nanometer-scale spatial information and nanosecond-scale temporal information. In this review, we briefly introduce the basic principles of FRET and assess the current state of progress in the development of new FRET techniques (such as FRET-FLIM, Homo-FRET and smFRET) for the analysis of plant membrane proteins. We also describe the various FRET-based biosensors used to quantify the homeostasis of signaling molecules and the active state of kinases. Furthermore, we summarize recent applications of these advanced FRET sensors in probing membrane protein interactions, stoichiometry, and protein clustering, which have shed light on the complex biological functions of membrane proteins in living plant cells.