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...

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Bibliographic Details
Published in:Structure (London) 2012-10, Vol.20 (10), p.1621-1628
Main Authors: Faelber, Katja, Held, Martin, Gao, Song, Posor, York, Haucke, Volker, Noé, Frank, Daumke, Oliver
Format: Article
Language:English
Subjects:
Animals
Catalytic Domain
Cell Membrane Structures - metabolism
Cell Membrane Structures - physiology
Dynamins - chemistry
Dynamins - physiology
Endocytosis
Humans
Models, Molecular
Protein Multimerization
Protein Structure, Quaternary
Protein Structure, Secondary
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Summary: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. Membrane scission is catalyzed by dynamin, a multi-domain mechano-chemical GTPase. Faelber et al. review structural and mechanistic aspects of helical dynamin filaments assembly, discuss their role in scission process, and propose a model for dynamin-mediated scission of membranes.
ISSN:0969-2126
1878-4186
DOI:10.1016/j.str.2012.08.028