Neural Wiskott Aldrich Syndrome Protein (N-WASP) and the Arp2/3 complex are recruited to sites of clathrin-mediated endocytosis in cultured fibroblasts
Neural Wiskott Aldrich Syndrome Protein (N-WASP) and the Arp2/3 complex are recruited to sites of clathrin-mediated endocytosis in cultured fibroblasts
复制标题
DOI：
10.1078/0171-9335-00356
复制
发表时间：
2004-02-01
影响因子：
6.6
通讯作者：
Almers, W
中科院分区：
文献类型：
--
作者：
Merrifield, CJ;Qualmann, B;Almers, W
一些研究结果表明，肌动蛋白介导的运动性在网格蛋白介导的内吞作用中可发挥作用，但目前尚不清楚该过程所需的关键蛋白质是否以及何时被招募到内吞位点。在此，我们利用双色消逝场显微镜技术在活的瑞士3T3细胞中研究这一问题。我们发现，在单个网格蛋白包被小窝内化时，Arp2/3复合物的一个组分Arp3会短暂出现。同时，还会有神经 - 威斯科特 - 奥尔德里奇综合征蛋白（N - WASP，一种已知的Arp2/3复合物激活剂）的额外招募。这两种蛋白质与肌动蛋白几乎同时出现。我们认为，N - WASP和Arp2/3复合物在网格蛋白介导的内吞作用的后期阶段触发肌动蛋白聚合，并将网格蛋白包被的小窝或囊泡从质膜推进到细胞质中。
Several findings suggest that actin-mediated motility can play a role in clathrin-mediated endocytosis but it remains unclear whether and when key proteins required for this process are recruited to endocytic sites. Here we investigate this question in live Swiss 3T3 cells using two-colour evanescent field (EF) microscopy. We rind that Arp3, a component of the Arp2/3 complex, appears transiently while single clathrin-coated pits internalize. There is also additional recruitment of Neural-Wiskott Aldrich Syndrome Protein (N-WASP), a known activator of the Arp2/3 complex. Both proteins appear at a ut the same time as actin. We suggest that N-WASP and the Arp2/3 complex trigger actin polymerization during a late step in clathrin-mediated endocytosis, and propel clathrin-coated pits or vesicles from the plasma membrane into the cytoplasm.