ArticleNature communications2018
Structural basis for membrane tethering by a bacterial dynamin-like pair.
Article in Nature communications, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
20 citing papers in PubMed, 39 citations in OpenAlex.
- Binding of Bacillus subtilis dynamin-like protein DynA to the bacterial membrane is essential for effective phage defense.The FEBS journal · 2026Article
- OPA1 mutations in dominant optic atrophy: domain-specific defects in mitochondrial fusion and apoptotic regulation.Journal of translational medicine · 2025Article
- Integrative modeling of guanylate binding protein dimers.Protein science : a publication of the Protein Society · 2023Article
- Dynamin-like proteins mediate extracellular vesicle secretion in Mycobacterium tuberculosis.EMBO reports · 2023Article
- SynDLP is a dynamin-like protein of Synechocystis sp. PCC 6803 with eukaryotic features.Nature communications · 2023Article
- Cyanobacterial membrane dynamics in the light of eukaryotic principles.Bioscience reports · 2023Article
- Reciprocal Regulation of Mitofusin 2-Mediated Mitophagy and Mitochondrial Fusion by Different PINK1 Phosphorylation Events.Frontiers in cell and developmental biology · 2022Article
- CryoEM structure of the super-constricted two-start dynamin 1 filament.Nature communications · 2021Article
- Dynamin controls neuropeptide secretion by organizing dense-core vesicle fusion sites.Science advances · 2021Article
- Review
- Phosphoinositide-binding proteins mark, shape and functionally modulate highly-diverged endocytic compartments in the parasitic protist Giardia lamblia.PLoS pathogens · 2020Article
- Bacterial dynamin-like protein DynA mediates lipid and content mixing.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2019Article
- Structural insights of human mitofusin-2 into mitochondrial fusion and CMT2A onset.Nature communications · 2019Article
- The structural biology of the dynamin-related proteins: New insights into a diverse, multitalented family.Traffic (Copenhagen, Denmark) · 2019Review
- A Molecular Perspective on Mitochondrial Membrane Fusion: From the Key Players to Oligomerization and Tethering of Mitofusin.The Journal of membrane biology · 2019Review
- Metabolic implications of organelle-mitochondria communication.EMBO reports · 2019Review
- Mycobacterial dynamin-like protein IniA mediates membrane fission.Nature communications · 2019Article
- Genetic dissection of Escherichia coli's master diguanylate cyclase DgcE: Role of the N-terminal MASE1 domain and direct signal input from a GTPase partner system.PLoS genetics · 2019Article
- Bacterial dynamin-like proteins reveal mechanism for membrane fusion.Nature communications · 2018Article
- Recent insights into the structure and function of Mitofusins in mitochondrial fusion.F1000Research · 2018Review
Corrections and comments
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Authors and funding
3 authors at 2 institutions in 2 countries.
Funding
Abstract
Dynamin-like proteins (DLPs) are large GTPases that restructure membrane. DLPs such as the mitofusins form heterotypic oligomers between isoform pairs that bridge and fuse opposing membranes. In bacteria, heterotypic oligomerisation may also be important for membrane remodelling as most DLP genes are paired within operons. How DLPs tether opposing membranes is unknown. Here we show the crystal structure of a DLP heterotypic pair from the pathogen Campylobacter jejuni. A 2:2 stoichiometric tetramer is observed where heterodimers, conjoined by a random coil linker, assemble back-to-back to form a tripartite DLP chain with extreme flexibility. In vitro, tetramerisation triggers GTPase activity and induces lipid binding. Liposomes are readily tethered and form tubes at high tetramer concentration. Our results provide a direct mechanism for the long-range binding and bridging of opposing membranes by a bacterial DLP pair. They also provide broad mechanistic and structural insights that are relevant to other heterotypic DLP complexes.
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Registered trials
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.