An endophilin-dynamin complex promotes budding of clathrin-coated vesicles during synaptic vesicle recycling
An endophilin-dynamin complex promotes budding of clathrin-coated vesicles during synaptic vesicle recycling
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DOI：
10.1242/jcs.072686
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发表时间：
2011-01-01
影响因子：
4
通讯作者：
Shupliakov, Oleg
中科院分区：
文献类型：
--
作者：
Sundborger, Anna;Soderblom, Cynthia;Shupliakov, Oleg
网格蛋白介导的囊泡在突触中的再循环是由一组独特的内吞蛋白和相互作用维持的。我们发现，在七鳃鳗突触的活动期间，内啡肽本地化的囊泡池在休息和螺旋网格蛋白包被的坑（CCP）的颈部。嗜内蛋白和发动蛋白共定位在网格蛋白外套的基部。在体外的脂质管上由这些蛋白质组成的蛋白质螺旋具有类似于在活突触中的CCP颈部处观察到的螺距，并且脂质管比单独由发动蛋白形成的那些更薄。在存在内嗜蛋白的情况下，微管形成效率和向脂管募集的发动蛋白的量显著增加。原位阻断内亲素SH3结构域的相互作用减少了发动蛋白在颈部的积累，并防止在GTP γ S存在下观察到的伸长颈部的形成。因此，内嗜蛋白将发动蛋白募集到CCP颈部的受限部分，形成复合物，其促进新突触囊泡的出芽。
Clathrin-mediated vesicle recycling in synapses is maintained by a unique set of endocytic proteins and interactions. We show that endophilin localizes in the vesicle pool at rest and in spirals at the necks of clathrin-coated pits (CCPs) during activity in lamprey synapses. Endophilin and dynamin colocalize at the base of the clathrin coat. Protein spirals composed of these proteins on lipid tubes in vitro have a pitch similar to the one observed at necks of CCPs in living synapses, and lipid tubules are thinner than those formed by dynamin alone. Tubulation efficiency and the amount of dynamin recruited to lipid tubes are dramatically increased in the presence of endophilin. Blocking the interactions of the endophilin SH3 domain in situ reduces dynamin accumulation at the neck and prevents the formation of elongated necks observed in the presence of GTP gamma S. Therefore, endophilin recruits dynamin to a restricted part of the CCP neck, forming a complex, which promotes budding of new synaptic vesicles.