ArticleNature communications2020
The hierarchical assembly of septins revealed by high-speed AFM.
Article in Nature communications, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 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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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
23 citing papers in PubMed, 59 citations in OpenAlex.
- High-Speed AFM Reveals Ligand-Dependent Supramolecular Switching of Human Phosphofructokinase-1.Research square · 2026Article
- Local RhoA activation induces anillin-independent septin recruitment in interphase cells.Molecular biology of the cell · 2026Article
- Lipid packing and local geometry influence septin curvature sensing.The Journal of cell biology · 2026Article
- Local RhoA activation induces septin recruitment.bioRxiv : the preprint server for biology · 2025Article
- Septin higher-order structure on yeast membranes in vitro.Nature communications · 2025Article
- Hexameric-Based Hierarchy in the Sizes of a Cytolysin Pore-Forming Complex.Biomolecules · 2025Article
- Capturing Dynamic Assembly of Nanoscale Proteins During Network Formation.Small (Weinheim an der Bergstrasse, Germany) · 2025Article
- A single septin from a polyextremotolerant yeast recapitulates many canonical functions of septin hetero-oligomers.Molecular biology of the cell · 2024Article
- X-ray structure of the metastable SEPT14-SEPT7 coiled coil reveals a hendecad region crucial for heterodimerization.Acta crystallographica. Section D, Structural biology · 2023Article
- Advanced imaging techniques for studying protein phase separation in living cells and at single-molecule level.Current opinion in chemical biology · 2023Review
- Small GTPase Cdc42, WASP, and scaffold proteins for higher-order assembly of the F-BAR domain protein.Science advances · 2023Article
- Spatiotemporal resolution in high-speed atomic force microscopy for studying biological macromolecules in action.Microscopy (Oxford, England) · 2023Review
- Curvature sensing as an emergent property of multiscale assembly of septins.Proceedings of the National Academy of Sciences of the United States of America · 2023Article
- Modeling membrane reshaping driven by dynamic protein assemblies.Current opinion in structural biology · 2023Review
- Probing both sides of the story.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- Tools shaping drug discovery and development.Biophysics reviews · 2022Review
- Perforin-2 clockwise hand-over-hand pre-pore to pore transition mechanism.Nature communications · 2022Article
- Article
- Hydration Dynamics and the Future of Small-Amplitude AFM Imaging in Air.Molecules (Basel, Switzerland) · 2021Article
- Revised subunit order of mammalian septin complexes explains their in vitro polymerization properties.Molecular biology of the cell · 2021Article
Corrections and comments
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Authors and funding
5 authors at 2 institutions in 1 country.
Funding
Abstract
Septins are GTP-binding proteins involved in diverse cellular processes including division and membrane remodeling. Septins form linear, palindromic heteromeric complexes that can assemble in filaments and higher-order structures. Structural studies revealed various septin architectures, but questions concerning assembly-dynamics and -pathways persist. Here we used high-speed atomic force microscopy (HS-AFM) and kinetic modeling which allowed us to determine that septin filament assembly was a diffusion-driven process, while formation of higher-order structures was complex and involved self-templating. Slightly acidic pH and increased monovalent ion concentrations favor filament-assembly, -alignment and -pairing. Filament-alignment and -pairing further favored diffusion-driven assembly. Pairing is mediated by the septin N-termini face, and may occur symmetrically or staggered, likely important for the formation of higher-order structures of different shapes. Multilayered structures are templated by the morphology of the underlying layers. The septin C-termini face, namely the C-terminal extension of Cdc12, may be involved in membrane binding.
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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 Socratic graph.