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首页> 外文期刊>Journal of Molecular Biology >A hinge in the distal end of the PACSIN 2 F-BAR domain may contribute to membrane-curvature sensing.
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A hinge in the distal end of the PACSIN 2 F-BAR domain may contribute to membrane-curvature sensing.

机译：PACSIN 2 F-BAR结构域远端的铰链可能有助于膜曲率检测。

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摘要

The protein kinase C and casein kinase 2 substrates in neurons (PACSINs) represent a subfamily of membrane-binding proteins characterized by an amino-terminal Bin-Amphiphysin-Rvs (F-BAR) domain. PACSINs link membrane trafficking with actin dynamics and regulate the localization of distinct cargo molecules. The F-BAR domain forms a dimer essential for lipid binding. We have obtained crystals of authentic murine PACSIN 2 that contain an ordered F-BAR domain, indicating that additional domains are flexibly connected to F-BAR. The structure shares similarity to other BAR domains and exhibits special features unique to PACSINs. These include the uneven distribution of charged residues on the concave molecular surface and a so-called wedge loop that is driven into the membrane upon binding of PACSIN. The murine PACSIN 2 F-BAR domain requires dimerization for sensing of curved membranes, and the present structure also provides a mechanism for higher-order oligomer formation. Importantly, comparison of murine with human and Drosophila PACSIN 2 F-BAR domains reveals stark differences in the orientation of distal helical segments leading to a wider crescent shape of murine PACSIN 2. We define hinge residues for these movements that may help PACSINs sense and concomitantly reinforce membrane curvature.
机译：神经元中的蛋白激酶C和酪蛋白激酶2底物（PACSIN）代表膜结合蛋白的亚家族，其特征在于氨基末端的Bin-Amphiphysin-Rvs（F-BAR）结构域。 PACSIN将膜运输与肌动蛋白动力学联系起来，并调节不同货物分子的定位。 F-BAR结构域形成脂质结合所必需的二聚体。我们已经获得了真实的鼠类PACSIN 2晶体，其中包含有序的F-BAR域，表明其他域可以灵活地连接到F-BAR。该结构与其他BAR域具有相似之处，并具有PACSIN特有的特殊功能。这些包括在凹形分子表面上带电残基的不均匀分布和所谓的楔形环，该楔形环在PACSIN结合后被驱动进入膜。鼠的PACSIN 2 F-BAR结构域需要二聚化以感测弯曲的膜，并且本结构还提供了高阶低聚物形成的机制。重要的是，将鼠类与人和果蝇的PACSIN 2 F-BAR结构域进行比较后发现，远端螺旋区段的方向存在明显差异，导致鼠PACSIN 2的月牙形更宽。我们为这些运动定义了铰链残基，这可能有助于PACSIN感知和伴随增强膜曲率。

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