ReviewBiopolymers2016
Invited review: Mechanisms of GTP hydrolysis and conformational transitions in the dynamin superfamily.
Review in Biopolymers, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 63 papers.
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Who cites it
63 citing papers in PubMed, 110 citations in OpenAlex.
- The molecular mechanisms of crista formation: how mitochondria give themselves breathing room.Biochemical Society transactions · 2026Review
- Structures of EHD2 filaments on curved membranes provide a model for caveolar neck stabilization.Nature communications · 2026Article
- Mechanistic insights into Ras-catalyzed GTP hydrolysis: conformational dynamics, catalytic mechanisms, and emerging therapeutic strategies.Biological chemistry · 2026Review
- Article
- Binding of Bacillus subtilis dynamin-like protein DynA to the bacterial membrane is essential for effective phage defense.The FEBS journal · 2026Article
- Conformational Rearrangement of Fission DSPs.BioEssays : news and reviews in molecular, cellular and developmental biology · 2025Review
- Structural basis of pseudoGTPase-mediated protein-protein interactions.Structure (London, England : 1993) · 2025Article
- Charcot-Marie-Tooth type 2A variants of mitofusin 2 sensitize cells to apoptotic cell death.Journal of cell science · 2025Article
- Structural and functional characterization of the brain-specific dynamin superfamily member RNF112.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Crystal structures reveal nucleotide-induced conformational changes in G motifs and distal regions in human guanylate-binding protein 2.Communications biology · 2025Article
- Mitofusin 2 displays fusion-independent roles in proteostasis surveillance.Nature communications · 2025Article
- Antiviral Mx proteins have an ancient origin and widespread distribution among eukaryotes.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- The Large GTPase Guanylate-Binding Protein-1 (GBP-1) Promotes Mitochondrial Fission in Glioblastoma.International journal of molecular sciences · 2024Article
- Antiviral Mx proteins have an ancient origin and widespread distribution among eukaryotes.bioRxiv : the preprint server for biology · 2024Article
- Identification of drug-like molecules targeting the ATPase activity of dynamin-like EHD4.PloS one · 2024Article
- Integrative modeling of guanylate binding protein dimers.Protein science : a publication of the Protein Society · 2023Article
- The Viral Protein Poly(A) Polymerase Catalytic Subunit Interacts with Guanylate-Binding Proteins 2 to Antagonize the Antiviral Ability of Targeting Ectromelia Virus.International journal of molecular sciences · 2023Article
- Guanylate-Binding Protein 2 Exerts GTPase-Dependent Anti-Ectromelia Virus Effect.Microorganisms · 2023Article
- ATPase activity of DFCP1 controls selective autophagy.Nature communications · 2023Article
- The large GTPase AtGBPL3 links nuclear envelope formation and morphogenesis to transcriptional repression.Nature plants · 2023Article
3 more citing papers are in PubMed but not listed here.
Corrections and comments
- Erratum issued
Authors and funding
2 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Dynamin superfamily proteins are multidomain mechano-chemical GTPases which are implicated in nucleotide-dependent membrane remodeling events. A prominent feature of these proteins is their assembly- stimulated mechanism of GTP hydrolysis. The molecular basis for this reaction has been initially clarified for the dynamin-related guanylate binding protein 1 (GBP1) and involves the transient dimerization of the GTPase domains in a parallel head-to-head fashion. A catalytic arginine finger from the phosphate binding (P-) loop is repositioned toward the nucleotide of the same molecule to stabilize the transition state of GTP hydrolysis. Dynamin uses a related dimerization-dependent mechanism, but instead of the catalytic arginine, a monovalent cation is involved in catalysis. Still another variation of the GTP hydrolysis mechanism has been revealed for the dynamin-like Irga6 which bears a glycine at the corresponding position in the P-loop. Here, we highlight conserved and divergent features of GTP hydrolysis in dynamin superfamily proteins and show how nucleotide binding and hydrolysis are converted into mechano-chemical movements. We also describe models how the energy of GTP hydrolysis can be harnessed for diverse membrane remodeling events, such as membrane fission or fusion. © 2016 Wiley Periodicals, Inc. Biopolymers 105: 580-593, 2016.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.