ArticleThe Journal of cell biology2020
Structural insights into G domain dimerization and pathogenic mutation of OPA1.
Article in The Journal of cell biology, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.
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Who cites it
27 citing papers in PubMed, 50 citations in OpenAlex.
- Review
- Structured illumination microscopy for high SNR 3D imaging from millimeter-thick tissues to cellular dynamics.Innovation (Cambridge (Mass.)) · 2026Article
- Super-Refractory Status Epilepticus (SRSE) in a Patient With Compound Heterozygous OPA1 Variants: Case Report and Literature Review.Annals of clinical and translational neurology · 2026Review
- MIRO1-mediated mitochondrial fusion is required for stomatal immunity in Arabidopsis.Nature plants · 2026Article
- OPA1 as a Cancer Target: Molecular Mechanisms, Structural Insights, and Strategies for Drug Development.Antioxidants (Basel, Switzerland) · 2026Review
- Molecular machineries shaping the mitochondrial inner membrane.Nature reviews. Molecular cell biology · 2025Review
- Small molecule OPA1 inhibitors amplify cytochrome c release and reverse cancer cells resistance to Bcl-2 inhibitors.Science advances · 2025Article
- Characterization of lncRNA-protein interactions associated with Prostate cancer and Androgen receptors by molecular docking simulations.Biochemistry and biophysics reports · 2025Article
- OPA1 mutations in dominant optic atrophy: domain-specific defects in mitochondrial fusion and apoptotic regulation.Journal of translational medicine · 2025Article
- Tetrahydrobenzimidazole TMQ0153 targets OPA1 and restores drug sensitivity in AML via ROS-induced mitochondrial metabolic reprogramming.Journal of experimental & clinical cancer research : CR · 2025Article
- Bringing together but staying apart: decisive differences in animal and fungal mitochondrial inner membrane fusion.Biological reviews of the Cambridge Philosophical Society · 2025Review
- Molecular mechanisms of mitochondrial dynamics.Nature reviews. Molecular cell biology · 2025Review
- Fast and deep phosphoproteome analysis with the Orbitrap Astral mass spectrometer.Nature communications · 2024Article
- Diabetes cardiomyopathy: targeted regulation of mitochondrial dysfunction and therapeutic potential of plant secondary metabolites.Frontiers in pharmacology · 2024Review
- Integrative modeling of guanylate binding protein dimers.Protein science : a publication of the Protein Society · 2023Article
- Article
- Article
- FGF21-FGFR1 controls mitochondrial homeostasis in cardiomyocytes by modulating the degradation of OPA1.Cell death & disease · 2023Article
- Article
- Mitochondrial dynamics proteins as emerging drug targets.Trends in pharmacological sciences · 2023Review
Corrections and comments
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Authors and funding
8 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The fusion of mammalian inner mitochondrial membranes (IMMs) is mediated by dynamin-like GTPase OPA1. Mutations in human OPA1 cause optic atrophy, but the molecular basis for membrane fusion and pathogenesis is not clear. Here, we determined the crystal structure of the minimal GTPase domain (MGD) of human OPA1. A three-helix bundle (HB) domain including two helices extending from the GTPase (G) domain and the last helix of OPA1 tightly associates with the G domain. In the presence of GDP and BeF3-, OPA1-MGD forms a dimer, the interface of which is critical for the maintenance of mitochondrial morphology. The catalytic core of OPA1 possesses unique features that are not present in other dynamin-like proteins. Biochemical experiments revealed that OPA1-MGD forms nucleotide-dependent dimers, which is important for membrane-stimulated GTP hydrolysis, and an N-terminal extension mediates nucleotide-independent dimerization that facilitates efficient membrane association. Our results suggest a multifaceted assembly of OPA1 and explain the effect of most OPA1 mutations on optic atrophy.
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