On the role of membrane anisotropy and BAR proteins in the stability of tubular membrane structures
On the role of membrane anisotropy and BAR proteins in the stability of tubular membrane structures
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DOI：
10.1016/j.jbiomech.2011.10.039
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发表时间：
2012-01-10
影响因子：
2.4
通讯作者：
Iglic, Ales
中科院分区：
文献类型：
--
作者：
Kabaso, Doron;Bobrovska, Nataliya;Iglic, Ales
最近的研究表明，肌动蛋白丝是不是至关重要的短期稳定性的管状膜突起起源于细胞表面。还已经证明，介导I-BAR蛋白的弯曲的纳米结构域和曲率可以解释膜突起的稳定性。在这里，我们构建了一个轴对称模型的膜突起，不包括肌动蛋白丝，以调查的贡献，在nanodomains（筏）和I-BAR蛋白的膜突起的稳定性。已经证明，Escherin纳米结构域和I-BAR蛋白可以仅在特定范围的自发曲率上稳定膜突起。另一方面，I-BAR蛋白的高自发曲率和/或高密度可导致系统不稳定和膜突起的径向方向上的不均匀收缩。与以前的研究一致，它也表明，各向同性的弯曲能的脂质是不足以解释所观察到的管状膜突起没有肌动蛋白丝的稳定性。(C)2011爱思唯尔有限公司保留所有权利。
Recent studies have demonstrated that actin filaments are not crucial for the short-term stability of tubular membrane protrusions originating from the cell surface. It has also been demonstrated that prominin nanodomains and curvature inducing I-BAR proteins could account for the stability of the membrane protrusion. Here we constructed an axisymmetric model of a membrane protrusion that excludes actin filaments in order to investigate the contributions of prominin nanodomains (rafts) and I-BAR proteins to the membrane protrusion stability. It was demonstrated that prominin nanodomains and I-BAR proteins can stabilize the membrane protrusion only over a specific range of spontaneous curvature. On the other hand, high spontaneous curvature and/or high density of I-BAR proteins could lead to system instability and to non-uniform contraction in the radial direction of the membrane protrusion. In agreement with previous studies, it was also shown that the isotropic bending energy of lipids is not sufficient to explain the stability of the observed tubular membrane protrusion without actin filaments. (C) 2011 Elsevier Ltd. All rights reserved.