Structural insights into dynamin-mediated membrane fission.
Dynamin is a multidomain mechanochemical guanine triphosphatase that catalyzes membrane scission, most notably of clathrin-coated endocytic vesicles. A number of recent publications have provided structural and mechanistic insights into the formation of helical dynamin filaments assembled by dynamic interactions of multiple domains within dynamin. As a prerequisite for membrane scission, this oligomer undergoes nucleotide-triggered large scale dynamic rearrangements. Here, we review these structural findings and discuss how the architecture of dynamin is poised for the assembly into right-handed helical filaments. Based on these data, we propose a structure-based model for dynamin-mediated scission of membranes.
Max-Delbrück-Centrum for Molecular Medicine, Crystallography, Robert-Rössle-Strasse 10, 13125 Berlin, Germany. katja.faelber@mdc-berlin.de
Katja
K
Faelber
Martin
M
Held
Song
S
Gao
York
Y
Posor
Volker
V
Haucke
Frank
F
Noé
Oliver
O
Daumke
D000818:Animals; D020134:Catalytic Domain; D021961:Cell Membrane Structures / Q000378:metabolism / Q000502:physiology; D034281:Dynamins / Q000737:chemistry* / Q000502:physiology; D004705:Endocytosis; D006801:Humans; D008958:Models, Molecular; D055503:Protein Multimerization; D020836:Protein Structure, Quaternary; D017433:Protein Structure, Secondary
D034281:Dynamins