The stalk region of dynamin drives the constriction of dynamin tubes

被引：115
作者：
Chen, YJ
Zhang, PJ
Egelman, EH [1 ]
Hinshaw, JE
机构：
[1] Univ Virginia, Dept Biochem & Mol Genet, Charlottesville, VA USA
[2] NIDDKD, Lab Cell Biochem & Biol, NIH, Bethesda, MD 20892 USA
来源：
NATURE STRUCTURAL & MOLECULAR BIOLOGY | 2004年 / 11卷 / 06期
基金：
美国国家卫生研究院;
关键词：
D O I：
10.1038/nsmb762
中图分类号：
Q5 [生物化学]; Q7 [分子生物学];
学科分类号：
071010 ; 081704 ;
摘要：
The GTPase dynamin is essential for numerous vesiculation events including clathrin-mediated endocytosis. Upon GTP hydrolysis, dynamin constricts a lipid bilayer. Previously, a three-dimensional structure of mutant dynamin in the constricted state was determined by helical reconstruction methods. We solved the nonconstricted state by a single-particle approach and show that the stalk region of dynamin undergoes a large conformational change that drives tube constriction.
引用
收藏
页码：574 / 575
页数：2
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