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首页> 外文期刊>Proceedings of the National Academy of Sciences of the United States of America >Loss of endocytic clathrin-coated pits upon acute depletion of phosphatidylinositol 4,5-bisphosphate
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Loss of endocytic clathrin-coated pits upon acute depletion of phosphatidylinositol 4,5-bisphosphate

机译：磷脂酰肌醇4,5-二磷酸酯的急性消耗会丢失内吞网格蛋白包被的小凹坑

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摘要

Phosphatidylinositol 4,5-bisphosphate [PI(4,5)P_2] a phosphoinositide concentrated predominantly in the plasma membrane, binds endocytic clathrin adaptors, many of their accessory factors, and a variety of actin-regulatory proteins. Here we have used fluorescent fusion proteins and total internal reflection fluorescence microscopy to investigate the effect of acute PI(4,5)P_2 breakdown on the dynamics of endocytic clathrin-coated pit components and of the actin regulatory complex, Arp2/3. PI(4,5)P_2 breakdown was achieved by the inducible recruitment to the plasma membrane of an inositol 5-phosphatase module through the rapamycin/FRB/FKBP system or by treatment with ionomycin. PI(4,5)P_2 depletion resulted in a dramatic loss of clathrin puncta, which correlated with a massive dissociation of endocytic adaptors from the plasma membrane. Remaining clathrin spots at the cell surface had only weak fluorescence and were static over time. Dynamin and the p20 subunit of the Arp2/3 actin regulatory complex, which were concentrated at late-stage clathrin-coated pits and in lamellipodia, also dissociated from the plasma membrane, and these changes correlated with an arrest of motility at the cell edge. These findings demonstrate the critical importance of PI(4,5)P_2 in clathrin coat dynamics and Arp2/3-dependent actin regulation.
机译：磷脂酰肌醇4,5-二磷酸[PI（4,5）P_2]主要集中在质膜中的磷酸肌醇，结合内吞网格蛋白衔接子，它们的许多辅助因子和多种肌动蛋白调节蛋白。在这里，我们已经使用荧光融合蛋白和全内反射荧光显微镜来研究急性PI（4,5）P_2分解对内吞网格蛋白包被的凹坑组件和肌动蛋白调节复合物Arp2 / 3动力学的影响。 PI（4,5）P_2的分解是通过雷帕霉素/ FRB / FKBP系统或通过离子霉素处理将肌醇5-磷酸酶模块诱导性募集到质膜上而实现的。 PI（4,5）P_2耗竭导致网格蛋白点的急剧损失，这与胞质衔接子从质膜的大量解离有关。细胞表面剩余的网格蛋白斑点仅具有弱荧光，并且随着时间的推移是静态的。 dynamin和Arp2 / 3肌动蛋白调节复合物的p20亚基也集中在后期网格蛋白包被的凹坑和片状脂膜中，也从质膜上解离，这些变化与细胞边缘的运动停滞有关。这些发现表明PI（4,5）P_2在网格蛋白外壳动力学和Arp2 / 3依赖肌动蛋白调节中至关重要。

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