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

doi:10.1074/jbc.C112.406769

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 journal › Article › peer-review

18 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 language	English
Pages (from-to)	36634-36638
Number of pages	5
Journal	Journal of Biological Chemistry
Volume	287
Issue number	44
DOIs	https://doi.org/10.1074/jbc.C112.406769
State	Published - 26 Oct 2012
Externally published	Yes

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

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.",

author = "Inbal Abutbul-Ionita and Jarungjit Rujiviphat and Iftach Nir and McQuibban, {G. Angus} and Dganit Danino",

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AU - Abutbul-Ionita, Inbal

AU - Rujiviphat, Jarungjit

AU - Nir, Iftach

AU - McQuibban, G. Angus

AU - Danino, Dganit

PY - 2012/10/26

Y1 - 2012/10/26

N2 - 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.

AB - 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.

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DO - 10.1074/jbc.C112.406769

M3 - 文章

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AN - SCOPUS:84868223334

SN - 0021-9258

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JO - Journal of Biological Chemistry

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

Abstract

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