Functional partnership between amphiphysin and dynamin in clathrin-mediated endocytosis

被引:510
作者
Takei, K
Slepnev, VI
Haucke, V
De Camilli, P
机构
[1] Yale Univ, Sch Med, Dept Cell Biol, New Haven, CT 06510 USA
[2] Yale Univ, Sch Med, Howard Hughes Med Inst, New Haven, CT 06510 USA
基金
美国国家卫生研究院;
关键词
D O I
10.1038/9004
中图分类号
Q2 [细胞生物学];
学科分类号
071009 ; 090102 ;
摘要
Amphiphysin, a protein that is highly concentrated in nerve terminals, has been proposed to function as a linker between the clathrin coat and dynamin in the endocytosis of synaptic vesicles. Here, using a cell-free system, we provide direct morphological evidence in support of this hypothesis. Unexpectedly, we also find that amphiphysin-1, like dynamin-1, can transform spherical liposomes into narrow tubules. Moreover, amphiphysin-1 assembles with dynamin-1 into ring-like structures around the tubules and enhances the liposome-fragmenting activity of dynamin-1 in the presence of GTP. These results show that amphiphysin binds lipid bilayers, indicate a potential function for amphiphysin in the changes in bilayer curvature that accompany vesicle budding, and imply a close functional partnership between amphiphysin and dynamin in endocytosis.
引用
收藏
页码:33 / 39
页数:7
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