AP2 接头可增强网格蛋白涂层的硬度。,The FEBS Journal

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AP2 接头可增强网格蛋白涂层的硬度。
The FEBS Journal ( IF 5.5 ) Pub Date : 2019-07-03 , DOI: 10.1111/febs.14961
Michael Lherbette ₁ , Lisa Redlingshöfer ₂ , Frances M Brodsky ₂ , Iwan A T Schaap ₁ , Philip N Dannhauser ₂

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质膜变形为网格蛋白包被的囊泡是网格蛋白介导的内吞作用的关键步骤，需要将网格蛋白和内吞适配器精心组装成膜相关的蛋白质外壳。这些膜弯曲和曲率稳定因素的个别作用受到当前争论的影响。因此，尚不清楚网格蛋白涂层本身是否足够坚硬以施加弯曲，如果是这样，是否可以通过连接接头蛋白有效地转移到膜上。我们最近证明，单独的网格蛋白就足以在体外形成膜芽。在这里，我们使用原子力显微镜来评估网格蛋白及其膜接头蛋白 2 (AP2) 对网格蛋白外壳刚度的贡献，这决定了囊泡形成的机制。我们发现网格蛋白涂层比它们所包围的膜硬不到 10 倍，这表明网格蛋白涂层形成所产生的力与膜弯曲所需的力之间存在微妙的平衡。我们观察到网格蛋白接头蛋白 AP2 增加了由天然网格蛋白形成的外壳的刚度，但不影响由缺乏轻链亚基的网格蛋白形成的弹性较差的外壳。因此，我们提出网格蛋白轻链对于网格蛋白外套的柔韧性很重要，并且 AP2 通过调节网格蛋白外套的硬度，在包被囊泡形成过程中促进有效的货物隔离。我们观察到网格蛋白接头蛋白 AP2 增加了由天然网格蛋白形成的外壳的刚度，但不影响由缺乏轻链亚基的网格蛋白形成的弹性较差的外壳。因此，我们提出网格蛋白轻链对于网格蛋白外套的柔韧性很重要，并且 AP2 通过调节网格蛋白外套的硬度，在包被囊泡形成过程中促进有效的货物隔离。我们观察到网格蛋白接头蛋白 AP2 增加了由天然网格蛋白形成的外壳的刚度，但不影响由缺乏轻链亚基的网格蛋白形成的弹性较差的外壳。因此，我们提出网格蛋白轻链对于网格蛋白外套的柔韧性很重要，并且 AP2 通过调节网格蛋白外套的硬度，在包被囊泡形成过程中促进有效的货物隔离。

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The AP2 adaptor enhances clathrin coat stiffness.

Deformation of the plasma membrane into clathrin-coated vesicles is a critical step in clathrin-mediated endocytosis and requires the orchestrated assembly of clathrin and endocytic adaptors into a membrane-associated protein coat. The individual role of these membrane-bending and curvature-stabilizing factors is subject to current debate. As such, it is unclear whether the clathrin coat itself is stiff enough to impose curvature and if so, whether this could be effectively transferred to the membrane by the linking adaptor proteins. We have recently demonstrated that clathrin alone is sufficient to form membrane buds in vitro. Here, we use atomic force microscopy to assess the contributions of clathrin and its membrane adaptor protein 2 (AP2) to clathrin coat stiffness, which determines the mechanics of vesicle formation. We found that clathrin coats are less than 10-fold stiffer than the membrane they enclose, suggesting a delicate balance between the forces harnessed from clathrin coat formation and those required for membrane bending. We observed that clathrin adaptor protein AP2 increased the stiffness of coats formed from native clathrin, but did not affect less-flexible coats formed from clathrin lacking the light chain subunits. We thus propose that clathrin light chains are important for clathrin coat flexibility and that AP2 facilitates efficient cargo sequestration during coated vesicle formation by modulating clathrin coat stiffness.

更新日期：2019-07-03

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