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Structure. 2012 Oct 10;20(10):1621-8. doi: 10.1016/j.str.2012.08.028.

Structural insights into dynamin-mediated membrane fission.

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Max-Delbrück-Centrum for Molecular Medicine, Crystallography, Robert-Rössle-Strasse 10, 13125 Berlin, Germany.


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.

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