Oligomerization of dynamin superfamily proteins in health and disease

Item Type:	Review
Title:	Oligomerization of dynamin superfamily proteins in health and disease
Creators Name:	Faelber, K. and Gao, S. and Held, M. and Posor, Y. and Haucke, V. and Noé, F. and Daumke, O.
Abstract:	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.
Keywords:	Dynamin Superfamily GTPases, Protein Structure, Membrane Remodeling, Oligomerization, Charcot-Marie-Tooth Disease, Centronuclear Myopathy, Animals
Source:	Progress in Molecular Biology and Translational Science
ISSN:	1877-1173
Publisher:	Elsevier / Academic Press
Volume:	117
Page Range:	411-443
Date:	2013
Official Publication:	https://doi.org/10.1016/B978-0-12-386931-9.00015-5
PubMed:	View item in PubMed

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