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首页> 外文期刊>Developmental cell >Structural insights into the organization of the cavin membrane coat complex.
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Structural insights into the organization of the cavin membrane coat complex.

机译：洞洞膜外套复合物组织的结构见解。

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摘要

Caveolae are cell-surface membrane invaginations that play critical roles in cellular processes including signaling and membrane homeostasis. The cavin proteins, in cooperation with caveolins, are essential for caveola formation. Here we show that a minimal N-terminal domain of the cavins, termed HR1, is required and sufficient for their homo- and hetero-oligomerization. Crystal structures of the mouse cavin1 and zebrafish cavin4a HR1 domains reveal highly conserved trimeric coiled-coil architectures, with intersubunit interactions that determine the specificity of cavin-cavin interactions. The HR1 domain contains a basic surface patch that interacts with polyphosphoinositides and coordinates with additional membrane-binding sites within the cavin C terminus to facilitate membrane association and remodeling. Electron microscopy of purified cavins reveals the existence of large assemblies, composed of a repeating rod-like structural element, and we propose that these structures polymerize through membrane-coupled interactions to form the unique striations observed on the surface of caveolae in?vivo.
机译：小窝是细胞表面膜的内陷，在信号传导和膜稳态等细胞过程中起关键作用。该cavin蛋白与caveolins协同作用，对caveola的形成至关重要。在这里，我们表明，cavins的最小N末端结构域（称为HR1）是必需的，并且对于它们的均聚和杂聚都是足够的。小鼠cavin1和斑马鱼cavin4a HR1域的晶体结构揭示了高度保守的三聚体卷曲螺旋结构，其亚基间相互作用决定了cavin-cavin相互作用的特异性。 HR1结构域包含一个基本的表面补丁，该补丁与多磷酸肌醇相互作用，并与cavin C末端内的其他膜结合位点配合，从而促进膜缔合和重塑。纯化腔管的电子显微镜检查揭示了大组件的存在，该组件由重复的棒状结构元素组成，我们建议这些结构通过膜耦合相互作用聚合，形成在体内小窝表面观察到的独特条纹。

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