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首页> 外文期刊>Developmental cell >An Organized Co-assembly of Clathrin Adaptors Is Essential for Endocytosis
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An Organized Co-assembly of Clathrin Adaptors Is Essential for Endocytosis

机译：网格蛋白适配器的有组织的组装对于胞吞作用必不可少

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摘要

Clathrin-mediated endocytosis, the main trafficking route from the plasma membrane to the cytoplasm, is critical to many fundamental cellular processes. Clathrin, coupled to the membrane by adaptor proteins, is thought to play a major structural role in endocytosis by self-assembling into a cage-like lattice around the forming vesicle. Although clathrin adaptors are essential for endocytosis, little is known about their structural role in this process. Here we show that the membrane-binding domains of two conserved clathrin adaptors, Sla2 and Ent1, co-assemble in a PI(4,5)P-2-dependent manner to form organized lattices on membranes. We determined the structure of the co-assembled lattice by electron cryo-microscopy and designed mutations that specifically impair the lattice formation in vitro. We show that these mutations block endocytosis in vivo. We suggest that clathrin adaptors not only link the polymerized clathrin to the membrane but also form an oligomeric structure, which is essential for membrane remodeling during endocytosis.
机译：网格蛋白介导的内吞作用是从质膜到细胞质的主要运输途径，对许多基本细胞过程至关重要。网格蛋白通过衔接蛋白与膜偶联，被认为通过自身组装成形成囊泡周围的笼状晶格而在胞吞作用中起主要结构作用。尽管网格蛋白衔接子对于内吞作用至关重要，但对其在这一过程中的结构作用知之甚少。在这里，我们显示了两个保守的网格蛋白衔接子Sla2和Ent1的膜结合域以PI（4,5）P-2依赖性方式共同组装，在膜上形成有组织的晶格。我们通过电子冷冻显微镜确定了共组装晶格的结构，并设计了一些突变，这些突变特别损害了体外的晶格形成。我们表明这些突变在体内阻止内吞。我们建议网格蛋白适配器不仅将聚合的网格蛋白连接到膜，而且还形成寡聚结构，这对于内吞过程中的膜重塑至关重要。

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