ArticleThe Journal of biological chemistry2017
The intrinsically disordered C-terminal linker of FtsZ regulates protofilament dynamics and superstructure
Article in The Journal of biological chemistry, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.
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Who cites it
22 citing papers in PubMed, 48 citations in OpenAlex.
- Methicillin treatment reveals that FtsZ phosphorylation influences the cell division ofPNAS nexus · 2026Article
- Functional flexibility in bacterial hub proteins is driven by proteome expansion.Scientific reports · 2026Article
- Comparative genomics andFrontiers in microbiology · 2026Article
- Article
- Crosslinking by ZapD drives the assembly of short FtsZ filaments into toroidal structures in solution.eLife · 2025Article
- The cell division protein FzlA performs a conserved function in diverse alphaproteobacteria.Journal of bacteriology · 2024Article
- GTPase activity regulates FtsZ ring positioning inMolecular biology of the cell · 2024Article
- N-terminus GTPase domain of the cytoskeleton protein FtsZ plays a critical role in its adaptation to high hydrostatic pressure.Frontiers in microbiology · 2024Article
- Insights into Membrane Curvature Sensing and Membrane Remodeling by Intrinsically Disordered Proteins and Protein Regions.The Journal of membrane biology · 2022Review
- FtsZ treadmilling is essential for Z-ring condensation and septal constriction initiation in Bacillus subtilis cell division.Nature communications · 2021Article
- Progression of the late-stage divisome is unaffected by the depletion of the cytoplasmic FtsZ pool.Communications biology · 2021Article
- FtsZ dynamics in bacterial division: What, how, and why?Current opinion in cell biology · 2021Review
- Cell Division Protein FtsZ Is Unfolded for N-Terminal Degradation by Antibiotic-Activated ClpP.mBio · 2020Article
- Insights into the Structure, Function, and Dynamics of the Bacterial Cytokinetic FtsZ-Ring.Annual review of biophysics · 2020Review
- Dissecting the Functional Contributions of the Intrinsically Disordered C-terminal Tail of Bacillus subtilis FtsZ.Journal of molecular biology · 2020Article
- Bacterial cell division at a glance.Journal of cell science · 2020Review
- FtsA Regulates Z-Ring Morphology and Cell Wall Metabolism in an FtsZ C-Terminal Linker-Dependent Manner in Caulobacter crescentus.Journal of bacteriology · 2020Article
- Regulation of cytokinesis: FtsZ and its accessory proteins.Current genetics · 2020Review
- At the Heart of Bacterial Cytokinesis: The Z Ring.Trends in microbiology · 2019Review
- Surface Orientation and Binding Strength Modulate Shape of FtsZ on Lipid Surfaces.International journal of molecular sciences · 2019Article
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
The bacterial tubulin FtsZ polymerizes to form a discontinuous ring that drives bacterial cell division by directing local cell wall synthesis. FtsZ comprises a polymerizing GTPase domain, an intrinsically disordered C-terminal linker (CTL), and a C-terminal conserved peptide (CTC). FtsZ protofilaments align circumferentially in the cell, with the CTC mediating attachment to membrane-associated division proteins. The assembly of FtsZ protofilaments into dynamic clusters is critical for cell division, but the interactions between protofilaments and regulatory mechanisms that mediate cluster assembly and dynamics are unknown. Here, we describe a role for the CTL of
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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.