Membrane partitioning and lipid selectivity of the N-terminal amphipathic H0 helices of endophilin isoforms.
Membrane partitioning and lipid selectivity of the N-terminal amphipathic H0 helices of endophilin isoforms.
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DOI：
10.1016/j.bbamem.2021.183660
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发表时间：
2021-10-01
期刊：
影响因子：
--
通讯作者：
Baumgart T
中科院分区：
文献类型：
--
作者：
Robustelli J;Baumgart T
内亲素是一种N-bar蛋白，其特征是具有一个新月形的杆状结构域和一个两亲性螺旋，有助于这些蛋白的膜结合。H0螺旋的确切功能一直是争论的话题。在哺乳动物中，有五种不同的内嗜素亚型，分为A(三个成员)和B(两个成员)亚类，它们在亚细胞定位和功能上有不同的描述。我们问这些成员的H0螺旋的分子性质在多大程度上影响它们的膜靶向行为。我们发现，内亲素异构体的所有H0螺旋都在无序和α-螺旋状态之间表现出两态平衡，其中螺旋二级结构可以通过三氟乙醇稳定。H0多肽在高TFE时的螺旋度有显著差异。我们通过圆二色谱监测二级结构的变化来研究H0膜的分配。我们发现，阴离子磷脂的存在是所有H0螺旋分配到膜中的关键。膜分配被发现对膜复杂性的变化很敏感。总体而言，H0B亚家族表现出比H0A亚家族更强的膜分配。H0A多肽与膜的结合主要通过静电相互作用进行。H0A亚家族之间的差异可能归因于氨基酸序列的轻微变化。同时，H0B亚家族对某些膜成分表现出更强的特异性，这可能将H0B多肽与内亲和素B的细胞功能联系起来。
Endophilin is an N-BAR protein, which is characterized by a crescent-shaped BAR domain and an amphipathic helix that contributes to the membrane binding of these proteins. The exact function of that H0 helix has been a topic of debate. In mammals, there are five different endophilin isoforms, grouped into A (three members) and B (two members) subclasses, which have been described to differ in their subcellular localization and function. We asked to what extent molecular properties of the H0 helices of these members affect their membrane targeting behavior. We found that all H0 helices of the endophilin isoforms display a two-state equilibrium between disordered and α-helical states in which the helical secondary structure can be stabilized through trifluoroethanol. The helicities in high TFE were strikingly different among the H0 peptides. We investigated H0-membrane partitioning by the monitoring of secondary structure changes via CD spectroscopy. We found that the presence of anionic phospholipids is critical for all H0 helices partitioning into membranes. Membrane partitioning is found to be sensitive to variations in membrane complexity. Overall, the H0 B subfamily displays stronger membrane partitioning than the H0 A subfamily. The H0 A peptide-membrane binding occurs predominantly through electrostatic interactions. Variation among the H0 A subfamily may be attributed to slight alterations in the amino acid sequence. Meanwhile, the H0 B subfamily displays greater specificity for certain membrane compositions, and this may link H0 B peptide binding to endophilin B’s cellular function.
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