Oligomerization of Dynamin Superfamily Proteins in Health and Disease

被引：41
作者：
Faelber, Katja [1 ]
Gao, Song [1 ,2 ]
Held, Martin [3 ]
Posor, York [4 ,5 ]
Haucke, Volker [4 ,5 ]
Noe, Frank [3 ]
Daumke, Oliver [1 ]
机构：
[1] Max Delbruck Ctr Mol Med, Berlin, Germany
[2] Sun Yat Sen Univ, Ctr Canc, State Key Lab Oncol South China, Guangzhou, Peoples R China
[3] Free Univ Berlin, Inst Math, Berlin, Germany
[4] Leibniz Inst Mol Pharmacol FMP, Berlin, Germany
[5] Free Univ Berlin, Berlin, Germany
来源：
OLIGOMERIZATION IN HEALTH AND DISEASE | 2013年 / 117卷
关键词：
SYNAPTIC VESICLE ENDOCYTOSIS; MARIE-TOOTH NEUROPATHY; DEPENDENT CONFORMATIONAL-CHANGES; CLATHRIN-MEDIATED ENDOCYTOSIS; PLECKSTRIN HOMOLOGY DOMAINS; MITOCHONDRIAL FISSION; CRYSTAL-STRUCTURE; STRUCTURAL BASIS; MAMMALIAN-CELLS; MEMBRANE FISSION;
D O I：
10.1016/B978-0-12-386931-9.00015-5
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：
Proteins of the dynamin superfamily are mechanochemical GTPases, which mediate nucleotide-dependent membrane remodeling events. The founding member dynamin is recruited to the neck of clathrin-coated endocytic vesicles where it oligomerizes into helical filaments. Nucleotide-hydrolysis-induced conformational changes in the oligomer catalyze scission of the vesicle neck. Here, we review recent insights into structure, function, and oligomerization of dynamin superfamily proteins and their roles in human diseases. We describe in detail the molecular mechanisms how dynamin oligomerizes at membranes and introduce a model how oligomerization is linked to membrane fission. Finally, we discuss molecular mechanisms how mutations in dynamin could lead to the congenital diseases, Centronuclear Myopathy and Charcot-Marie Tooth disease.
引用
收藏
页码：411 / 443
页数：33
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