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We began analyzing https://journals.biologists.com/jcs/article/117/26/6535/3004/Mitofusin-1-and-2-play-distinct-roles-in, but it redirected us to https://journals.biologists.com/jcs/article/117/26/6535/3004/Mitofusin-1-and-2-play-distinct-roles-in. The analysis below is for the second page.

Title[redir]:
Mitofusin 1 and 2 play distinct roles in mitochondrial fusion reactions via GTPase activity | Journal of Cell Science | The Company of Biologists
Description:
The mammalian homologues of yeast and Drosophila Fzo, mitofusin (Mfn) 1 and 2, are both essential for mitochondrial fusion and maintenance of mitochondrial morphology. Though the GTPase domain is required for Mfn protein function, the molecular mechanisms of the GTPase-dependent reaction as well as the functional division of the two Mfn proteins are unknown. To examine the function of Mfn proteins, tethering of mitochondrial membranes was measured in vitro by fluorescence microscopy using green fluorescence protein- or red fluorescent protein-tagged and Mfn1-expressing mitochondria, or by immunoprecipitation using mitochondria harboring HA- or FLAG-tagged Mfn proteins. These experiments revealed that Mfn1-harboring mitochondria were efficiently tethered in a GTP-dependent manner, whereas Mfn2-harboring mitochondria were tethered with only low efficiency. Sucrose density gradient centrifugation followed by co-immunoprecipitation revealed that Mfn1 produced oligomerized ∼250 kDa and ∼450 kDa complexes in a GTP-dependent manner. The ∼450 kDa complex contained oligomerized Mfn1 from distinct apposing membranes (docking complex), whereas the ∼250 kDa complex was composed of Mfn1 present on the same membrane or in the membrane-solubilized state (cis complex). These results were also confirmed using blue-native PAGE. Mfn1 exhibited higher activity for this reaction than Mfn2. Purified recombinant Mfn1 exhibited ∼eightfold higher GTPase activity than Mfn2. These findings indicate that the two Mfn proteins have distinct activities, and suggest that Mfn1 is mainly responsible for GTP-dependent membrane tethering.

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mfn, open, menu, cell, journal, article, mitochondrial, mitochondria, biology, search, sign, company, register, issue, gtpase, activity, proteins, membranes, kda, complex, membrane, alert, content, science, contacts, distinct, fusion, mechanisms, microscopy, gtpdependent, biologists, jcs, decision, manuscript, imaging, policy, registered, skip, input, suggest, journals, articles, december, mitofusin, author, information, share, icon, tools, fzo,

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open menu red fluorescent protein-tagged cell science journal article research article fast-tracked decision making jcs fast-track option flag-tagged mfn proteins gtp-dependent membrane tethering gtp-dependent manner journals journal gtpase activity search purchase naotada ishihara blue-native page google scholar crossref cambridge cb24 9lf mfn1-expressing mitochondria mfn1-harboring mitochondria green fluorescence protein �cell biology cell biology guest editors ana gtpase-dependent reaction membrane-solubilized state prokaryotic intracytoplasmic membranes mitochondria harboring ha distinct apposing membranes company limited mfn protein function skip article information molecular mechanisms mitochondrial fusion reactions fluorescence microscopy suggest view access $30 mfn2-harboring mitochondria ��250 kda complex institution sign permissions sign rights reserved company mfn1 present special issue cell sci manuscripts ��450 kda complexes gtpase domain content register

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      author:
            name:Ishihara, Naotada
            affiliation:Department of Molecular Biology, Graduate School of Medical Science, Kyushu University, Fukuoka 812-8582, Japan
            type:Person
            name:Eura, Yuka
            affiliation:Department of Molecular Biology, Graduate School of Medical Science, Kyushu University, Fukuoka 812-8582, Japan
            type:Person
            name:Mihara, Katsuyoshi
            affiliation:Department of Molecular Biology, Graduate School of Medical Science, Kyushu University, Fukuoka 812-8582, Japan
            type:Person
      description:The mammalian homologues of yeast and Drosophila Fzo, mitofusin (Mfn) 1 and 2, are both essential for mitochondrial fusion and maintenance of mitochondrial morphology. Though the GTPase domain is required for Mfn protein function, the molecular mechanisms of the GTPase-dependent reaction as well as the functional division of the two Mfn proteins are unknown. To examine the function of Mfn proteins, tethering of mitochondrial membranes was measured in vitro by fluorescence microscopy using green fluorescence protein- or red fluorescent protein-tagged and Mfn1-expressing mitochondria, or by immunoprecipitation using mitochondria harboring HA- or FLAG-tagged Mfn proteins. These experiments revealed that Mfn1-harboring mitochondria were efficiently tethered in a GTP-dependent manner, whereas Mfn2-harboring mitochondria were tethered with only low efficiency. Sucrose density gradient centrifugation followed by co-immunoprecipitation revealed that Mfn1 produced oligomerized ∼250 kDa and ∼450 kDa complexes in a GTP-dependent manner. The ∼450 kDa complex contained oligomerized Mfn1 from distinct apposing membranes (docking complex), whereas the ∼250 kDa complex was composed of Mfn1 present on the same membrane or in the membrane-solubilized state (cis complex). These results were also confirmed using blue-native PAGE. Mfn1 exhibited higher activity for this reaction than Mfn2. Purified recombinant Mfn1 exhibited ∼eightfold higher GTPase activity than Mfn2. These findings indicate that the two Mfn proteins have distinct activities, and suggest that Mfn1 is mainly responsible for GTP-dependent membrane tethering.
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      headline:Mitofusin 1 and 2 play distinct roles in mitochondrial fusion reactions via GTPase activity
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      affiliation:Department of Molecular Biology, Graduate School of Medical Science, Kyushu University, Fukuoka 812-8582, Japan
      name:Mihara, Katsuyoshi
      affiliation:Department of Molecular Biology, Graduate School of Medical Science, Kyushu University, Fukuoka 812-8582, Japan

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