Curvature dependence of BAR protein membrane association and dissociation kinetics.
Curvature dependence of BAR protein membrane association and dissociation kinetics.
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DOI：
10.1038/s41598-022-11221-9
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发表时间：
2022-05-10
影响因子：
4.6
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中科院分区：
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BAR（Bin/Amphiphysin/Rvs）结构域蛋白作为脂质双层弯曲器和曲率传感器发挥功能，并且它们有助于参与细胞信号传导和代谢的膜成形。通过平衡结合和动力学研究，研究了它们的膜形状传感机制。在以前的研究中，停流光谱已被用来推断出一个积极的依赖膜曲率的结合速率常数，kon，一个BAR蛋白质称为endophilin。然而，体扩散的内亲和素，对动力学结合参数的影响尚未得到彻底考虑。采用类似的方法，并使用多种大小的脂质囊泡，我们得到了一个线性依赖的kon囊泡曲率。然而，我们发现，所观察到的关系，可以解释不考虑局部曲率的敏感能力，在膜协会的过程中的内啡肽。与此相反，从停流测量获得的扩散无关的解结合速率常数（koff）显示出对膜曲率的负依赖性，这是由内亲蛋白-膜相互作用控制/介导的。后一种依赖性，除了蛋白质-蛋白质相互作用的膜，解释了选择性结合的BAR蛋白高度弯曲的膜在平衡结合实验。
BAR (Bin/Amphiphysin/Rvs) domain containing proteins function as lipid bilayer benders and curvature sensors, and they contribute to membrane shaping involved in cell signaling and metabolism. The mechanism for their membrane shape sensing has been investigated by both equilibrium binding and kinetic studies. In prior research, stopped-flow spectroscopy has been used to deduce a positive dependence on membrane curvature for the binding rate constant, kon, of a BAR protein called endophilin. However, the impact of bulk diffusion of endophilin, on the kinetic binding parameters has not been thoroughly considered. Employing similar methods, and using lipid vesicles of multiple sizes, we obtained a linear dependence of kon on vesicle curvature. However, we found that the observed relation can be explained without considering the local curvature sensing ability of endophilin in the membrane association process. In contrast, the diffusion-independent unbinding rate constant (koff) obtained from stopped-flow measurements shows a negative dependence on membrane curvature, which is controlled/mediated by endophilin-membrane interactions. This latter dependency, in addition to protein–protein interactions on the membrane, explains the selective binding of BAR proteins to highly curved membranes in equilibrium binding experiments.
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