Structural insights into dynamin-mediated membrane fission.

Katja Faelber, Martin Held, Song Gao, York Posor, Volker Haucke, Frank Noé, Oliver Daumke

Max-Delbrück-Centrum for Molecular Medicine, Crystallography, Robert-Rössle-Strasse 10, 13125 Berlin, Germany. katja.faelber@mdc-berlin.de

Structure (London, England : 1993) 2012 Oct 10

filter terms:

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. Copyright © 2012 Elsevier Ltd. All rights reserved.

Citation

Katja Faelber, Martin Held, Song Gao, York Posor, Volker Haucke, Frank Noé, Oliver Daumke. Structural insights into dynamin-mediated membrane fission. Structure (London, England : 1993). 2012 Oct 10;20(10):1621-8