Structural insights into dynamin-mediated membrane fission

Item Type:	Review
Title:	Structural insights into dynamin-mediated membrane fission
Creators Name:	Faelber, K. and Held, M. and Gao, S. and Posor, Y. and Haucke, V. and Noe, F. and Daumke, O.
Abstract:	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.
Keywords:	Catalytic Domain, Cell Membrane Structures, Dynamins, Endocytosis, Molecular Models, Protein Multimerization, Protein Structure, Animals
Source:	Structure
ISSN:	0969-2126
Publisher:	Cell Press
Volume:	20
Number:	10
Page Range:	1621-1628
Date:	10 October 2012
Official Publication:	https://doi.org/10.1016/j.str.2012.08.028
PubMed:	View item in PubMed

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