Conformational changes in Dnm1 support a contractile mechanism for mitochondrial fission

Jason A. Mears, Laura L. Lackner, Shunming Fang, Elena Ingerman, Jodi Nunnari, Jenny E. Hinshaw

Research output: Contribution to journalArticle

253 Scopus citations

Abstract

Mitochondria are dynamic organelles that undergo cycles of fission and fusion. The yeast dynamin-related protein Dnm1 has been localized to sites of mitochondrial division. Using cryo-EM, we have determined the three-dimensional (3D) structure of Dnm1 in a GTP-bound state. The 3D map showed that Dnm1 adopted a unique helical assembly when compared with dynamin, which is involved in vesicle scission during endocytosis. Upon GTP hydrolysis, Dnm1 constricted liposomes and subsequently dissociated from the lipid bilayer. The magnitude of Dnm1 constriction was substantially larger than the decrease in diameter previously reported for dynamin. We postulate that the larger conformational change is mediated by a flexible Dnm1 structure that has limited interaction with the underlying bilayer. Our structural studies support the idea that Dnm1 has a mechanochemical role during mitochondrial division.

Original languageEnglish (US)
Pages (from-to)20-27
Number of pages8
JournalNature Structural and Molecular Biology
Volume18
Issue number1
DOIs
StatePublished - Jan 1 2011

ASJC Scopus subject areas

  • Structural Biology
  • Molecular Biology

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