Structural Insights into the Mechanism of Dynamin Superfamily Proteins

被引：98

作者：

Jimah, John R. ^{[1
]}

Hinshaw, Jenny E. ^{[1
]}

机构：

[1] NIDDK, Struct Cell Biol Sect, Lab Cell & Mol Biol, NIH, Bethesda, MD 20892 USA

来源：

TRENDS IN CELL BIOLOGY | 2019年 / 29卷 / 03期

关键词：

PLECKSTRIN HOMOLOGY DOMAIN; GUANYLATE-BINDING PROTEIN-1; DEPENDENT CONFORMATIONAL-CHANGES; GTP-BINDING; MITOCHONDRIAL FUSION; CRYSTAL-STRUCTURE; ENDOPLASMIC-RETICULUM; MECHANOCHEMICAL ENZYME; NUCLEOTIDE-BINDING; HOMOTYPIC FUSION;

D O I：

10.1016/j.tcb.2018.11.003

中图分类号：

Q2 [细胞生物学];

学科分类号：

071009 ; 090102 ;

摘要：

Dynamin superfamily proteins (DSPs) mediate membrane fission and fusion necessary for endocytosis, organelle biogenesis and maintenance, as well as for bacterial cytokinesis. They also function in the innate immune response to pathogens and in organizing the cytoskeleton. In this review, we summarize the current understanding of the molecular mechanism of DSPs, with emphasis on the structural basis of function. Studies from the past decade on the structure and mechanism of DSPs enable comparative analysis of shared mechanisms and unique features of this protein family.

引用

页码：257 / 273

页数：17

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