title: Oligomerization of dynamin superfamily proteins in health and disease.
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.
authors.affiliation: Max-Delbrück-Centrum for Molecular Medicine, Crystallography, Berlin, Germany.
authors.forename: Katja
authors.initials: K
authors.lastname: Faelber
authors.forename: Song
authors.initials: S
authors.lastname: Gao
authors.forename: Martin
authors.initials: M
authors.lastname: Held
authors.forename: York
authors.initials: Y
authors.lastname: Posor
authors.forename: Volker
authors.initials: V
authors.lastname: Haucke
authors.forename: Frank
authors.initials: F
authors.lastname: Noé
authors.forename: Oliver
authors.initials: O
authors.lastname: Daumke
mesh_terms: D000818:Animals; D004194:Disease / Q000235:genetics; D034281:Dynamins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D006262:Health; D006801:Humans; D008958:Models, Molecular; D009154:Mutation / Q000235:genetics; D055503:Protein Multimerization
chemical_list: D034281:Dynamins