SH3-domain-containing proteins function at distinct steps in clathrin-coated vesicle formation
SH3-domain-containing proteins function at distinct steps in clathrin-coated vesicle formation
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DOI：
10.1038/10091
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发表时间：
1999-06-01
影响因子：
21.3
通讯作者：
Schmid, SL
中科院分区：
文献类型：
--
作者：
Simpson, F;Hussain, NK;Schmid, SL
几种含有SH 3结构域的蛋白质因与发动蛋白的相互作用而参与内吞作用;然而，它们的功能尚未确定。在这里，我们报告的有效重建的ATP，GTP，胞质溶胶和动力蛋白依赖的形成网格蛋白包被的囊泡透化3 T3-L1细胞。intersectin、endophilin I、syndapin I和amphiphysin II的SH 3结构域通过与膜相关蛋白的相互作用在体外抑制包被囊泡的形成。大多数测试的SH 3域选择性地抑制涉及膜分裂的晚期事件，但相交蛋白的SH 3A域独特地抑制中间事件，导致形成收缩的涂层凹坑。这些结果表明，SH 3结构域和他们的合作伙伴之间的相互作用功能顺序内吞包被囊泡的形成。
Several SH3-domain-containing proteins have been implicated in endocytosis by virtue of their interactions with dynamin; however, their functions remain undefined. Here we report the efficient reconstitution of ATP-, GTP-, cytosol- and dynamin-dependent formation of clathrin-coated vesicles in permeabilized 3T3-L1 cells. The SH3 domains of intersectin, endophilin I, syndapin I and amphiphysin II inhibit coated-vesicle formation in vitro through interactions with membrane-associated proteins. Most of the SH3 domains tested selectively inhibit late events involving membrane fission, but the SH3A domain of intersectin uniquely inhibits intermediate events leading to the formation of constricted coated pits. These results suggest that interactions between SH3 domains and their partners function sequentially in endocytic coated-vesicle formation.