The stalk region of dynamin drives the constriction of dynamin tubes
The stalk region of dynamin drives the constriction of dynamin tubes
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DOI：
10.1038/nsmb762
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发表时间：
2004-06-01
影响因子：
16.8
通讯作者：
Hinshaw, JE
中科院分区：
文献类型：
--
作者：
Chen, YJ;Zhang, PJ;Hinshaw, JE
GTPase动力蛋白对许多囊泡事件至关重要，包括网格蛋白介导的内吞作用。在GTP水解时，动力蛋白收缩脂质双分子层。以前，突变体动力蛋白在收缩状态下的三维结构是通过螺旋重建方法确定的。我们用单粒子方法解决了非收缩状态，并表明动力蛋白的柄区经历了一个大的构象变化，驱动管收缩。
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.