Evidence map›Paper›PMID 29280220›Full record

ArticleMolecular microbiology2018

FtsA reshapes membrane architecture and remodels the Z-ring in Escherichia coli.

Joseph Conti, Marissa G Viola, Jodi L Camberg

Open access · bronzeAbstract read
In one paragraph

Article in Molecular microbiology, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.

0numbers the graph read from it
0cells of the map it votes in
29citing papers in PubMed
5.3field-weighted citation impact, top 4% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

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.

2 · The registry

The trial behind it

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.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

29 citing papers in PubMed, 53 citations in OpenAlex.

  1. High-throughput discovery of inhibitory protein fragments with AlphaFold.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  2. Article
  3. High-throughput discovery of inhibitory protein fragments with AlphaFold.bioRxiv : the preprint server for biology · 2024
    Article
  4. Review
  5. Building the Bacterial Divisome at the Septum.Sub-cellular biochemistry · 2024
    Review
  6. Article
  7. Review
  8. Article
  9. Article
  10. Review
  11. Review
  12. Article
  13. FtsZ dynamics in bacterial division: What, how, and why?Current opinion in cell biology · 2021
    Review
  14. Article
  15. Control of septum thickness by the curvature of SepF polymers.Proceedings of the National Academy of Sciences of the United States of America · 2021
    Article
  16. Article
  17. Review
  18. Article
  19. Article
  20. Review
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

3 authors at 1 institution in 1 country.

Joseph ContiDepartments of Cell and Molecular Biology.
Marissa G ViolaDepartments of Cell and Molecular Biology.
Jodi L CambergDepartments of Cell and Molecular Biology.ORCID 0000-0002-8838-4461
University of Rhode Island · US

Funding

Mechanism of Cell Division in ProkaryotesR01GM118927 · NIGMS · UNIVERSITY OF RHODE ISLAND · PI CAMBERG, JODI LYNN · 2017 to 2021
$1.4M
NIGMS NIH HHS R01 GM118927
6 · The paper itself

Abstract

Cell division in prokaryotes initiates with assembly of the Z-ring at midcell, which, in Escherichia coli, is tethered to the inner leaflet of the cytoplasmic membrane through a direct interaction with FtsA, a widely conserved actin homolog. The Z-ring is comprised of polymers of tubulin-like FtsZ and has been suggested to provide the force for constriction. Here, we demonstrate that FtsA exerts force on membranes causing redistribution of membrane architecture, robustly hydrolyzes ATP and directly engages FtsZ polymers in a reconstituted system. Phospholipid reorganization by FtsA occurs rapidly and is mediated by insertion of a C-terminal membrane targeting sequence (MTS) into the bilayer and further promoted by a nucleotide-dependent conformational change relayed to the MTS. FtsA also recruits FtsZ to phospholipid vesicles via a direct interaction with the FtsZ C-terminus and regulates FtsZ assembly kinetics. These results implicate the actin homolog FtsA in establishment of a Z-ring scaffold, while directly remodeling the membrane and provide mechanistic insight into localized cell wall remodeling, invagination and constriction at the onset of division.

Indexed as

Adenosine TriphosphateBacterial ProteinsCell Cycle ProteinsCell DivisionCell MembraneCytoskeletal ProteinsEscherichia coliEscherichia coli ProteinsExtracellular VesiclesHydrolysisLipid DropletsMutagenesis, Site-DirectedPhospholipidsAdenosine TriphosphateBacterial ProteinsCell Cycle ProteinsCytoskeletal ProteinsEscherichia coli ProteinsFtsA protein, E coliFtsZ protein, BacteriaPhospholipids

Identifiers

PMID29280220
PMCPMC5796856
OpenAlexW2779046686

What OpenQuestion holds

Textmetadata
LicenceTDM
Read underepoch 390

Registered trials

None linked

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.