Dynamin-dependent vesicle twist at the final stage of clathrin-mediated endocytosis

被引:43
|
作者
Cheng, Xiaodong [1 ,2 ]
Chen, Kuangcai [1 ]
Dong, Bin [1 ]
Yang, Meek [1 ]
Filbrun, Seth L. [1 ]
Myoung, Yong [1 ]
Huang, Teng-Xiang [1 ]
Gu, Yan [3 ]
Wang, Gufeng [1 ]
Fang, Ning [1 ,2 ]
机构
[1] Georgia State Univ, Dept Chem, Atlanta, GA 30303 USA
[2] Xiamen Univ, Coll Chem & Chem Engn, Innovat Lab Sci & Technol Energy Mat Fujian Prov, State Key Lab Phys Chem Solid Surfaces, Xiamen, Peoples R China
[3] Bristol Myers Squibb Co, Devens, MA USA
关键词
DOMAIN-CONTAINING PROTEINS; MEMBRANE FISSION; DRUG-DELIVERY; CONSTRICTION; RECRUITMENT; GTPASE; ACTIN; AMPHIPHYSIN; ORIENTATION; SCISSION;
D O I
10.1038/s41556-021-00713-x
中图分类号
Q2 [细胞生物学];
学科分类号
071009 ; 090102 ;
摘要
Dynamin has an important role in clathrin-mediated endocytosis by cutting the neck of nascent vesicles from the cell membrane. Here, using gold nanorods as cargos to image dynamin action during live clathrin-mediated endocytosis, we show that, near the peak of dynamin accumulation, the cargo-containing vesicles always exhibit abrupt, right-handed rotations that finish in a short time (-0.28 s). The large and quick twist, herein named the super twist, is the result of the coordinated dynamin helix action upon GTP hydrolysis. After the super twist, the rotational freedom of the vesicle increases substantially, accompanied by simultaneous or delayed translational movement, indicating that it detaches from the cell membrane. These observations suggest that dynamin-mediated scission involves a large torque generated by the coordinated actions of multiple dynamins in the helix, which is the main driving force for vesicle scission.
引用
收藏
页码:859 / +
页数:23
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