ArticleScientific reports2017
A membrane-inserted structural model of the yeast mitofusin Fzo1.
Article in Scientific reports, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.
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Who cites it
15 citing papers in PubMed, 28 citations in OpenAlex.
- E4 ubiquitin ligase promotes mitofusin turnover and mitochondrial stress response.Molecular cell · 2023Article
- Docking and stability defects in mitofusin highlight the proteasome as a potential therapeutic target.iScience · 2023Article
- A dominant negative mitofusin causes mitochondrial perinuclear clusters because of aberrant tethering.Life science alliance · 2023Article
- Mitochondrial Surveillance by Cdc48/p97: MAD vs. Membrane Fusion.International journal of molecular sciences · 2020Review
- Defective nucleotide-dependent assembly and membrane fusion in Mfn2 CMT2A variants improved by Bax.Life science alliance · 2020Article
- Dual role of a GTPase conformational switch for membrane fusion by mitofusin ubiquitylation.Life science alliance · 2020Article
- Plasticity in salt bridge allows fusion-competent ubiquitylation of mitofusins and Cdc48 recognition.Life science alliance · 2019Article
- Structural dataset from microsecond-long simulations of yeast mitofusin Fzo1 in the context of membrane docking.Data in brief · 2019Article
- A Molecular Perspective on Mitochondrial Membrane Fusion: From the Key Players to Oligomerization and Tethering of Mitofusin.The Journal of membrane biology · 2019Review
- Rsp5 and Mdm30 reshape the mitochondrial network in response to age-induced vacuole stress.Molecular biology of the cell · 2019Article
- Structural basis for membrane tethering by a bacterial dynamin-like pair.Nature communications · 2018Article
- Structure of a mitochondrial fission dynamin in the closed conformation.Nature structural & molecular biology · 2018Article
- Systematic mapping of contact sites reveals tethers and a function for the peroxisome-mitochondria contact.Nature communications · 2018Article
- Recent insights into the structure and function of Mitofusins in mitochondrial fusion.F1000Research · 2018Review
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Authors and funding
6 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Mitofusins are large transmembrane GTPases of the dynamin-related protein family, and are required for the tethering and fusion of mitochondrial outer membranes. Their full-length structures remain unknown, which is a limiting factor in the study of outer membrane fusion. We investigated the structure and dynamics of the yeast mitofusin Fzo1 through a hybrid computational and experimental approach, combining molecular modelling and all-atom molecular dynamics simulations in a lipid bilayer with site-directed mutagenesis and in vivo functional assays. The predicted architecture of Fzo1 improves upon the current domain annotation, with a precise description of the helical spans linked by flexible hinges, which are likely of functional significance. In vivo site-directed mutagenesis validates salient aspects of this model, notably, the long-distance contacts and residues participating in hinges. GDP is predicted to interact with Fzo1 through the G1 and G4 motifs of the GTPase domain. The model reveals structural determinants critical for protein function, including regions that may be involved in GTPase domain-dependent rearrangements.
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