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首页> 外文期刊>Trends in Cell Biology >Bar domain proteins: a role in tubulation, scission and actin assembly in clathrin-mediated endocytosis
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Bar domain proteins: a role in tubulation, scission and actin assembly in clathrin-mediated endocytosis

机译:棒域蛋白:在网格蛋白介导的内吞作用中的输卵管,分裂和肌动蛋白组装中的作用

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摘要

Endocytosis is an important way for cells to take up liquids and particles from their environment. It requires membrane bending to be coupled with membrane fission, and the actin cytoskeleton has an active role in membrane remodelling. Here, we review recent research into the function of Bin-Amphiphysin-Rvs (BAR) domain proteins, which can sense membrane curvature and recruit actin to membranes. BAR proteins interact with the endocytic and cytoskeletal machinery, including the GTPase dynamin (which mediates vesicle fission), N-WASP (an Arp2/3 complex regulator) and synaptojanin (a phosphoinositide phosphatase). We describe three classes of BAR domains, BAR, N-BAR and F-BAR, providing examples of each discussing and how they function in linking membranes to the actin cytoskeleton in endocytosis.
机译:胞吞作用是细胞从其环境吸收液体和颗粒的重要途径。它要求膜弯曲与膜裂变结合,并且肌动蛋白细胞骨架在膜重塑中具有积极作用。在这里,我们回顾最近对Bin-Amphiphysin-Rvs(BAR)域蛋白功能的研究,该蛋白可以感知膜曲率并向膜募集肌动蛋白。 BAR蛋白与内吞和细胞骨架机制相互作用,包括GTPase动力蛋白(介导囊泡裂变),N-WASP(Arp2 / 3复合调节剂)和突触蛋白(磷酸肌醇磷酸酶)。我们描述了三类BAR结构域:BAR,N-BAR和F-BAR,提供了每个讨论的示例,以及它们如何在内吞作用中将膜连接到肌动蛋白细胞骨架上发挥作用。

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