ReviewMolecular microbiology2023
Anchors: A way for FtsZ filaments to stay membrane bound.
Review in Molecular microbiology, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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Who cites it
14 citing papers in PubMed, 18 citations in OpenAlex.
- Defining the order of assembly of theJournal of bacteriology · 2026Article
- Molecular Mechanism of the SepF N‑Terminal Conformational Switch in Ring Assembly and Membrane Anchoring.JACS Au · 2026Article
- Article
- Transcriptional Analysis of Cell Division-Related Genes inMicroorganisms · 2026Article
- Control of cell division by anbioRxiv : the preprint server for biology · 2026Article
- Defining the order of assembly of thebioRxiv : the preprint server for biology · 2026Article
- Cooperative and divergent properties of bacterial actin isoforms inBiophysics and physicobiology · 2026Article
- Distinct cell division features inJournal of bacteriology · 2025Review
- Identification of SepF in Streptococcus suis involving cell division.BMC microbiology · 2025Article
- A Predicted Helix-Turn-Helix Core Is Critical for Bacteriophage Kil Peptide to DisruptAntibiotics (Basel, Switzerland) · 2025Article
- GpsB interacts with FtsZ in multiple species and may serve as an accessory Z-ring anchor.Molecular biology of the cell · 2025Article
- The divisome is a self-enhancing machine in Escherichia coli and Caulobacter crescentus.Nature communications · 2024Article
- Article
- Role of the antiparallel double-stranded filament form of FtsA in activating thebioRxiv : the preprint server for biology · 2024Article
Corrections and comments
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Authors and funding
3 authors at 2 institutions in 1 country.
Funding
Abstract
Most bacteria use the tubulin homolog FtsZ to organize their cell division. FtsZ polymers initially assemble into mobile complexes that circle around a ring-like structure at the cell midpoint, followed by the recruitment of other proteins that will constrict the cytoplasmic membrane and synthesize septal peptidoglycan to divide the cell. Despite the need for FtsZ polymers to associate with the membrane, FtsZ lacks intrinsic membrane binding ability. Consequently, FtsZ polymers have evolved to interact with the membrane through adaptor proteins that both bind FtsZ and the membrane. Here, we discuss recent progress in understanding the functions of these FtsZ membrane tethers. Some, such as FtsA and SepF, are widely conserved and assemble into varied oligomeric structures bound to the membrane through an amphipathic helix. Other less-conserved proteins, such as EzrA and ZipA, have transmembrane domains, make extended structures, and seem to bind to FtsZ through two separate interactions. This review emphasizes that most FtsZs use multiple membrane tethers with overlapping functions, which not only attach FtsZ polymers to the membrane but also organize them in specific higher-order structures that can optimize cell division activity. We discuss gaps in our knowledge of these concepts and how future studies can address them.
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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.