Membrane tethering and nucleotide-dependent conformational changes drive mitochondrial genome maintenance (Mgm1) protein-mediated membrane fusion

Inbal Abutbul-Ionita, Jarungjit Rujiviphat, Iftach Nir, G. Angus McQuibban*, Dganit Danino

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

14 Scopus citations

Abstract

Background: Dynamin proteins shape membranes by promoting membrane curvature, fission, and fusion. Results: Cryo-EM demonstrates how the dynamin-related protein Mgm1 assembles onto and tethers membranes followed by nucleotide-dependent conformational changes. Conclusion: Mgm1 may mediate mitochondrial fusion by bridging opposing membranes and undergoing structural transitions. Significance: This study provides new mechanistic details of how dynamins may function as fusion molecules.

Original languageEnglish
Pages (from-to)36634-36638
Number of pages5
JournalJournal of Biological Chemistry
Volume287
Issue number44
DOIs
StatePublished - 26 Oct 2012

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