Dynamin architecture - from monomer to polymer

被引：31

作者：

Low, Harry H. ^{[1
]}

Loewe, Jan ^{[1
]}

机构：

[1] MRC Lab Mol Biol, Cambridge CB2 0QH, England

来源：

CURRENT OPINION IN STRUCTURAL BIOLOGY | 2010年 / 20卷 / 06期

基金：

英国生物技术与生命科学研究理事会; 英国医学研究理事会;

关键词：

DEPENDENT CONFORMATIONAL-CHANGES; GUANYLATE-BINDING PROTEIN-1; CRYSTAL-STRUCTURE; GTPASE-ACTIVITY; MITOCHONDRIAL FUSION; STRUCTURAL BASIS; STALK REGION; MECHANISM; DOMAIN; MEMBRANE;

D O I：

10.1016/j.sbi.2010.09.011

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：

Dynamins form a family of eukaryotic and prokaryotic proteins involved in membrane fission, fusion and restructuring. They have complex mechanisms of self-assembly, which are coupled to the tubulation and destabilization of lipid bilayers. Recent structural data has revolutionized our understanding and is now yielding detailed insights into dynamin structure, from monomer through to polymer. Traditional division of the dynamin subunit into GTPase domain, middle domain and GTPase effector domain based on sequence alignments and biochemistry is not supported by recent structural data. A unified model of dynamin architecture is presented here, based on observation that the basic dynamin fold is conserved across evolutionary kingdoms.

引用

收藏

页码：791 / 798

页数：8

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