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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 (U.S.A.)
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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