AP-2 recruitment to synaptotagmin stimulated by tyrosine-based endocytic motifs
AP-2 recruitment to synaptotagmin stimulated by tyrosine-based endocytic motifs
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DOI：
10.1126/science.285.5431.1268
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发表时间：
1999-08-20
期刊：
影响因子：
56.9
通讯作者：
De Camilli, P
中科院分区：
文献类型：
--
作者：
Haucke, V;De Camilli, P
网状蛋白介导的内吞作用是通过网状蛋白接头蛋白AP-2被募集到质膜上而启动的，在质膜上突触素被认为是一个对接位置。AP-2还与存在于其他货物蛋白中的内吞模体相互作用。具有酪氨酸内吞基序的多肽刺激AP-2与突触素的结合，并促进AP-2募集到神经元和非神经元细胞的质膜。这提示了一种机制，通过这种机制，负载货物蛋白可以刺激笼状蛋白包被的凹坑的成核。
Clathrin-mediated endocytosis is initiated by the recruitment of the clathrin adaptor protein AP-2 to the plasma membrane where the membrane protein synaptotagmin is thought to act as a docking site. AP-2 also interacts with endocytic motifs present in other cargo proteins. Peptides with a tyrosine-based endocytic motif stimulated binding of AP-2 to synaptotagmin and enhanced AP-2 recruitment to the plasma membrane of neuronal and non-neuronal cells. This suggests a mechanism by which nucleation of clathrin-coated pits is stimulated by the loading of cargo proteins.