Structural insights into dynamin-mediated membrane fission

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


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.

Publication types

  • Research Support, Non-U.S. Gov't
  • Review

MeSH terms

  • 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


  • Dynamins