Fusion of the endoplasmic reticulum by membrane-bound GTPases

被引：56

作者：

Hu, Junjie ^{[1
]}

Rapoport, Tom A. ^{[2
,3
]}

机构：

[1] Chinese Acad Sci, Inst Biophys, Natl Lab Biomacromol, Beijing 100101, Peoples R China

[2] Harvard Med Sch, Howard Hughes Med Inst, Boston, MA 02115 USA

[3] Harvard Med Sch, Dept Cell Biol, Boston, MA 02115 USA

来源：

SEMINARS IN CELL & DEVELOPMENTAL BIOLOGY | 2016年 / 60卷

关键词：

Endoplasmic reticulum; Membrane fusion; Atlastin; HOMOTYPIC ER FUSION; NETWORK FORMATION; PROTEIN ATLASTIN; STRUCTURAL BASIS; GOLGI-APPARATUS; PROVIDE INSIGHT; C-TERMINUS; SNARE; SEY1P; GTP;

D O I：

10.1016/j.semcdb.2016.06.001

中图分类号：

Q2 [细胞生物学];

学科分类号：

071009 ; 090102 ;

摘要：

The endoplasmic reticulum (ER) membrane forms an elaborate network of tubules and sheets that is continuously remodeled. This dynamic behavior requires membrane fusion that is mediated by dynamin-like GTPases: the atlastins in metazoans and Sey1p and related proteins in yeast and plants. Crystal structures of the cytosolic domains of these membrane proteins and biochemical experiments can now be integrated into a model that explains many aspects of the molecular mechanism by which these membrane-bound GTPases mediate membrane fusion. (C) 2016 Elsevier Ltd. All rights reserved.

引用

页码：105 / 111

页数：7

共 55 条

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