ArticleMolecular biology of the cell2009
An intramolecular signaling element that modulates dynamin function in vitro and in vivo.
Article in Molecular biology of the cell, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 58 papers.
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Who cites it
58 citing papers in PubMed.
- Conformational Rearrangement of Fission DSPs.BioEssays : news and reviews in molecular, cellular and developmental biology · 2025Review
- SLC-25A46 regulates mitochondrial fusion through the mitofusin protein FZO-1 and is essential for maintaining neuronal morphology.Journal of cell science · 2025Article
- Molecular mechanisms of mitochondrial dynamics.Nature reviews. Molecular cell biology · 2025Review
- Cryo-EM structures of membrane-bound dynamin in a post-hydrolysis state primed for membrane fission.Developmental cell · 2024Article
- Multifaceted functions of Drp1 in hypoxia/ischemia-induced mitochondrial quality imbalance: from regulatory mechanism to targeted therapeutic strategy.Military Medical Research · 2023Review
- DNM2 levels normalization improves muscle phenotypes of a novel mouse model for moderate centronuclear myopathy.Molecular therapy. Nucleic acids · 2023Article
- A dog model for centronuclear myopathy carrying the most common DNM2 mutation.Disease models & mechanisms · 2022Article
- The hypervariable region of atlastin-1 is a site for intrinsic and extrinsic regulation.The Journal of cell biology · 2021Article
- Quantification and demonstration of the collective constriction-by-ratchet mechanism in the dynamin molecular motor.Proceedings of the National Academy of Sciences of the United States of America · 2021Article
- Role of Clathrin and Dynamin in Clathrin Mediated Endocytosis/Synaptic Vesicle Recycling and Implications in Neurological Diseases.Frontiers in cellular neuroscience · 2021Review
- Structural and functional characterization of the dominant negative P-loop lysine mutation in the dynamin superfamily protein Vps1.Protein science : a publication of the Protein Society · 2020Article
- The cell biology of mitochondrial membrane dynamics.Nature reviews. Molecular cell biology · 2020Review
- Affinity Purification and Functional Characterization of Dynamin-Related Protein 1.Methods in molecular biology (Clifton, N.J.) · 2020Article
- The structural biology of the dynamin-related proteins: New insights into a diverse, multitalented family.Traffic (Copenhagen, Denmark) · 2019Review
- Structural Insights into the Mechanism of Dynamin Superfamily Proteins.Trends in cell biology · 2019Review
- Dynamin 2 (DNM2) as Cause of, and Modifier for, Human Neuromuscular Disease.Neurotherapeutics : the journal of the American Society for Experimental NeuroTherapeutics · 2018Review
- Structures of the fungal dynamin-related protein Vps1 reveal a unique, open helical architecture.The Journal of cell biology · 2018Article
- Steric interference from intrinsically disordered regions controls dynamin-related protein 1 self-assembly during mitochondrial fission.Scientific reports · 2018Article
- Dynamin-Like Proteins Are Potentially Involved in Membrane Dynamics within Chloroplasts and Cyanobacteria.Frontiers in plant science · 2018Article
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6 authors.
Funding
Abstract
Dynamin exhibits a high basal rate of GTP hydrolysis that is enhanced by self-assembly on a lipid template. Dynamin's GTPase effector domain (GED) is required for this stimulation, though its mechanism of action is poorly understood. Recent structural work has suggested that GED may physically dock with the GTPase domain to exert its stimulatory effects. To examine how these interactions activate dynamin, we engineered a minimal GTPase-GED fusion protein (GG) that reconstitutes dynamin's basal GTPase activity and utilized it to define the structural framework that mediates GED's association with the GTPase domain. Chemical cross-linking of GG and mutagenesis of full-length dynamin establishes that the GTPase-GED interface is comprised of the N- and C-terminal helices of the GTPase domain and the C-terminus of GED. We further show that this interface is essential for structural stability in full-length dynamin. Finally, we identify mutations in this interface that disrupt assembly-stimulated GTP hydrolysis and dynamin-catalyzed membrane fission in vitro and impair the late stages of clathrin-mediated endocytosis in vivo. These data suggest that the components of the GTPase-GED interface act as an intramolecular signaling module, which we term the bundle signaling element, that can modulate dynamin function in vitro and in vivo.
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Registered trials
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