Role of phosphorylation in regulation of the assembly of endocytic coat complexes
Role of phosphorylation in regulation of the assembly of endocytic coat complexes
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DOI：
10.1126/science.281.5378.821
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发表时间：
1998-08-07
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：
Slepnev, VI;Ochoa, GC;De Camilli, P
网格蛋白介导的内吞作用涉及网格蛋白外壳组分及其辅助蛋白的组装和分解循环。大鼠脑提取物的去磷酸化显示出促进发动蛋白1、突触Janin 1和两栖physin组装成还包括网格蛋白和AP-2的复合物。发动蛋白1和突触Janin 1的磷酸化抑制它们与两栖physin的结合，而两栖physin的磷酸化抑制其与AP-2和网格蛋白的结合。因此，磷酸化调节的协会和解离周期的网格蛋白为基础的内吞机制，和钙依赖性去磷酸化的内吞蛋白质可以准备神经末梢的内吞爆发。
Clathrin-mediated endocytosis involves cycles of assembly and disassembly of clathrin coat components and their accessory proteins. Dephosphorylation of rat brain extract was shown to promote the assembly of dynamin 1, synaptojanin 1, and amphiphysin into complexes that also included clathrin and AP-2, Phosphorylation of dynamin 1 and synaptojanin 1 inhibited their binding to amphiphysin, whereas phosphorylation of amphiphysin inhibited its binding to AP-2 and clathrin. Thus, phosphorylation regulates the association and dissociation cycle of the clathrin-based endocytic machinery, and calcium-dependent dephosphorylation of endocytic proteins could prepare nerve terminals for a burst of endocytosis.