ArticleScientific reports2018
Steric interference from intrinsically disordered regions controls dynamin-related protein 1 self-assembly during mitochondrial fission.
Article in Scientific reports, 2018. 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.
- Dysregulation of liquid-liquid phase separation: from molecular mechanisms to targeted therapies in cardiovascular diseases.Journal of nanobiotechnology · 2026Review
- AGPAT2 acts at the crossroads of lipid biosynthesis and DRP1-mediated ER morphogenesis.Nature communications · 2025Article
- Conformational Rearrangement of Fission DSPs.BioEssays : news and reviews in molecular, cellular and developmental biology · 2025Review
- Mitochondrial fission - changing perspectives for future progress.Journal of cell science · 2025Review
- Membrane Association of Intrinsically Disordered Proteins.Annual review of biophysics · 2025Review
- Acute diacylglycerol production activates critical membrane-shaping proteins leading to mitochondrial tubulation and fission.Nature communications · 2025Article
- Molecular mechanisms of mitochondrial dynamics.Nature reviews. Molecular cell biology · 2025Review
- Drp1: Focus on Diseases Triggered by the Mitochondrial Pathway.Cell biochemistry and biophysics · 2024Review
- Structural basis for regulated assembly of the mitochondrial fission GTPase Drp1.Nature communications · 2024Article
- Allosteric control of dynamin-related protein 1 through a disordered C-terminal Short Linear Motif.Nature communications · 2024Article
- DRP1: At the Crossroads of Dysregulated Mitochondrial Dynamics and Altered Cell Signaling in Cancer Cells.ACS omega · 2023Review
- The variable domain from dynamin-related protein 1 promotes liquid-liquid phase separation that enhances its interaction with cardiolipin-containing membranes.Protein science : a publication of the Protein Society · 2023Article
- Disease-associated mutations in Drp1 have fundamentally different effects on the mitochondrial fission machinery.Human molecular genetics · 2023Article
- The Drp1-Mediated Mitochondrial Fission Protein Interactome as an Emerging Core Player in Mitochondrial Dynamics and Cardiovascular Disease Therapy.International journal of molecular sciences · 2023Review
- Article
- Drp1 and the cytoskeleton: mechanistic nexus in mitochondrial division.Current opinion in physiology · 2022Article
- Mitochondrial dynamics and its impact on human health and diseases: inside the DRP1 blackbox.Journal of molecular medicine (Berlin, Germany) · 2022Review
- Mitochondrial dynamics involves molecular and mechanical events in motility, fusion and fission.Frontiers in cell and developmental biology · 2022Review
- Mff oligomerization is required for Drp1 activation and synergy with actin filaments during mitochondrial division.Molecular biology of the cell · 2021Article
- PathogenicGenes · 2021Article
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Authors and funding
10 authors.
Funding
Abstract
The self-assembling, mechanoenzymatic dynamin superfamily GTPase, dynamin-related protein 1 (Drp1), catalyzes mitochondrial and peroxisomal fission. Distinct intrinsically disordered regions (IDRs) in Drp1 substitute for the canonical pleckstrin homology (PH) domain and proline-rich domain (PRD) of prototypical dynamin, which cooperatively regulate endocytic vesicle scission. Whether the Drp1 IDRs function analogously to the corresponding dynamin domains however remains unknown. We show that an IDR unique to the Drp1 GTPase (G) domain, the 'extended 80-loop', albeit dissimilar in location, structure, and mechanism, functions akin to the dynamin PRD by enabling stable Drp1 mitochondrial recruitment and by suppressing Drp1 cooperative GTPase activity in the absence of specific partner-protein interactions. Correspondingly, we find that another IDR, the Drp1 variable domain (VD), in conjunction with the conserved stalk L1N loop, functions akin to the dynamin PH domain; first, in an 'auto-inhibitory' capacity that restricts Drp1 activity through a long-range steric inhibition of helical inter-rung G-domain dimerization, and second, as a 'fulcrum' for Drp1 self-assembly in the proper helical register. We show that the Drp1 VD is necessary and sufficient for specific Drp1-phospholipid interactions. We further demonstrate that the membrane-dependent VD conformational rearrangement essential for the alleviation of Drp1 auto-inhibition is contingent upon the basal GTP hydrolysis-dependent generation of Drp1 dimers from oligomers in solution. IDRs thus conformationally couple the enzymatic and membrane activities of Drp1 toward membrane fission.
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