The stalk region of dynamin drives the constriction of dynamin tubes

被引：114

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

页码：574 / 575

页数：2

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