期刊
STRUCTURE
卷 20, 期 10, 页码 1621-1628出版社
CELL PRESS
DOI: 10.1016/j.str.2012.08.028
关键词
-
资金
- German Research Foundation [SFB 740, SFB958]
- International Human Frontier Science Program Organization
- EMBO Young Investigator Program
Dynamin is a multidomain mechanochemical guanine triphosphatase that catalyzes membrane scission, most notably of clathrin-coated endocytic vesicles. A number of recent publications have provided structural and mechanistic insights into the formation of helical dynamin filaments assembled by dynamic interactions of multiple domains within dynamin. As a prerequisite for membrane scission, this oligomer undergoes nucleotide-triggered large scale dynamic rearrangements. Here, we review these structural findings and discuss how the architecture of dynamin is poised for the assembly into right-handed helical filaments. Based on these data, we propose a structure-based model for dynamin-mediated scission of membranes.
作者
我是这篇论文的作者
点击您的名字以认领此论文并将其添加到您的个人资料中。
推荐
暂无数据