Dynamin, a membrane-remodelling GTPase

被引：748

作者：

Ferguson, Shawn M. ^{[1
,2
]}

De Camilli, Pietro ^{[1
,2
,3
,4
]}

机构：

[1] Yale Univ, Sch Med, Dept Cell Biol, New Haven, CT 06510 USA

[2] Yale Univ, Sch Med, Program Cellular Neurosci Neurodegenerat & Repair, New Haven, CT 06510 USA

[3] Yale Univ, Sch Med, Kavli Inst Neurosci, New Haven, CT 06510 USA

[4] Yale Univ, Sch Med, Howard Hughes Med Inst, New Haven, CT 06510 USA

来源：

NATURE REVIEWS MOLECULAR CELL BIOLOGY | 2012年 / 13卷 / 02期

基金：

美国国家卫生研究院;

关键词：

CLATHRIN-COATED PITS; PLECKSTRIN HOMOLOGY DOMAIN; RECEPTOR-MEDIATED ENDOCYTOSIS; ACTIN CYTOSKELETON; MECHANOCHEMICAL ENZYME; STRUCTURAL BASIS; MOLECULAR-MECHANISM; AMPHIPHYSIN-2; BIN1; VESICLE FORMATION; HOMOTYPIC FUSION;

D O I：

10.1038/nrm3266

中图分类号：

Q2 [细胞生物学];

学科分类号：

071009 ; 090102 ;

摘要：

Dynamin, the founding member of a family of dynamin-like proteins (DLPs) implicated in membrane remodelling, has a critical role in endocytic membrane fission events. The use of complementary approaches, including live-cell imaging, cell-free studies, X-ray crystallography and genetic studies in mice, has greatly advanced our understanding of the mechanisms by which dynamin acts, its essential roles in cell physiology and the specific function of different dynamin isoforms. In addition, several connections between dynamin and human disease have also emerged, highlighting specific contributions of this GTPase to the physiology of different tissues.

引用

页码：75 / 88

页数：14

共 194 条

[31] Dynamin GTPase domain mutants block endocytic vesicle formation at morphologically distinct stages [J].