ArticleNature cell biology2014
The bacterial cell division proteins FtsA and FtsZ self-organize into dynamic cytoskeletal patterns.
Article in Nature cell biology, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 177 papers.
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Who cites it
177 citing papers in PubMed.
- Automated synthetic cell-based screening for designed proteins with emergent functions.Nature communications · 2026Article
- The penicillin-binding protein PBP1b fortifies the Escherichia coli division site against osmotic rupture.Nature microbiology · 2026Article
- The transcription factor Vca0578 (DsvR) mediated expression of ZapC is required to promote cell division during lytic transglycosylase insufficiency inbioRxiv : the preprint server for biology · 2026Article
- Optimizing spatial organization of FtsZ rings for large-scale constriction in synthetic cells.Nature communications · 2026Article
- Elucidating chiral myosin-induced actin dynamics: From single-filament behavior to collective structures.Proceedings of the National Academy of Sciences of the United States of America · 2026Article
- Extensile Active Hydrogels Driven by Living FtsZ Polymers.Small (Weinheim an der Bergstrasse, Germany) · 2026Article
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- Crosslinking by ZapD drives the assembly of short FtsZ filaments into toroidal structures in solution.eLife · 2025Article
- Distinct cell division features inJournal of bacteriology · 2025Review
- Membrane Association of Intrinsically Disordered Proteins.Annual review of biophysics · 2025Review
- Differential GTP-dependent in-vitro polymerization of recombinant Physcomitrella FtsZ proteins.Scientific reports · 2025Article
- Complex state transitions of the bacterial cell division protein FtsZ.Molecular biology of the cell · 2024Article
- Stay on track - revelations of bacterial cell wall synthesis enzymes and things that go by single-molecule imaging.Current opinion in microbiology · 2024Review
- Cell constriction requires processive septal peptidoglycan synthase movement independent of FtsZ treadmilling in Staphylococcus aureus.Nature microbiology · 2024Article
- Collective motion of chiral particles in complex noise environments.The European physical journal. E, Soft matter · 2024Article
- Manipulating Microbial Cell Morphology for the Sustainable Production of Biopolymers.Polymers · 2024Review
- Self-organization of mortal filaments and its role in bacterial division ring formation.Nature physics · 2024Article
- Insights into the assembly and regulation of the bacterial divisome.Nature reviews. Microbiology · 2024Review
- Building the Bacterial Divisome at the Septum.Sub-cellular biochemistry · 2024Review
117 more citing papers are in PubMed but not listed here.
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2 authors.
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Abstract
Bacterial cytokinesis is commonly initiated by the Z-ring, a cytoskeletal structure that assembles at the site of division. Its primary component is FtsZ, a tubulin superfamily GTPase, which is recruited to the membrane by the actin-related protein FtsA. Both proteins are required for the formation of the Z-ring, but if and how they influence each other's assembly dynamics is not known. Here, we reconstituted FtsA-dependent recruitment of FtsZ polymers to supported membranes, where both proteins self-organize into complex patterns, such as fast-moving filament bundles and chirally rotating rings. Using fluorescence microscopy and biochemical perturbations, we found that these large-scale rearrangements of FtsZ emerge from its polymerization dynamics and a dual, antagonistic role of FtsA: recruitment of FtsZ filaments to the membrane and negative regulation of FtsZ organization. Our findings provide a model for the initial steps of bacterial cell division and illustrate how dynamic polymers can self-organize into large-scale structures.
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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.