Evidence map›Paper›PMID 29119622›Full record

ArticleMolecular microbiology2018

FzlA, an essential regulator of FtsZ filament curvature, controls constriction rate during Caulobacter division.

Patrick J Lariviere, Piotr Szwedziak, Christopher R Mahone, Jan Löwe, Erin D Goley

Open access · hybridAbstract 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 18 papers.

0numbers the graph read from it
0cells of the map it votes in
18citing papers in PubMed
3.1field-weighted citation impact, top 8% 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

18 citing papers in PubMed, 35 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. GTPase activity regulates FtsZ ring positioning inMolecular biology of the cell · 2024
    Article
  6. Article
  7. Article
  8. Article
  9. Plasticity in the cell division processes of obligate intracellular bacteria.Frontiers in cellular and infection microbiology · 2023
    Review
  10. FtsZ dynamics in bacterial division: What, how, and why?Current opinion in cell biology · 2021
    Review
  11. Article
  12. Bacterial cell division at a glance.Journal of cell science · 2020
    Review
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
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

5 authors at 2 institutions in 2 countries.

Patrick J LariviereDepartment of Biological Chemistry, Johns Hopkins University School of Medicine, Baltimore, MD, 21205, USA.
Piotr SzwedziakStructural Studies Division, MRC Laboratory of Molecular Biology, Cambridge, CB20QH, UK.
Christopher R MahoneDepartment of Biological Chemistry, Johns Hopkins University School of Medicine, Baltimore, MD, 21205, USA.
Jan LöweStructural Studies Division, MRC Laboratory of Molecular Biology, Cambridge, CB20QH, UK.
Erin D GoleyDepartment of Biological Chemistry, Johns Hopkins University School of Medicine, Baltimore, MD, 21205, USA.ORCID 0000-0002-8518-2303
Johns Hopkins University · USMRC Laboratory of Molecular Biology · GB

Funding

BIOCHEMISTRY, CELLULAR AND MOLECULAR BIOLOGY PROGRAMT32GM007445 · NIGMS · JOHNS HOPKINS UNIVERSITY · PI GREEN, RACHEL · 1985 to 2021
$24.1M
Regulation and Mechanism of the C. Crescentus Cytokinetic RingR01GM108640 · NIGMS · JOHNS HOPKINS UNIVERSITY · PI GOLEY, ERIN D · 2015 to 2019
$1.6M
Medical Research Council MC_U105184326Medical Research Council U105184326NIGMS NIH HHS R01 GM108640NIGMS NIH HHS T32 GM007445
6 · The paper itself

Abstract

During bacterial division, polymers of the tubulin-like GTPase FtsZ assemble at midcell to form the cytokinetic Z-ring, which coordinates peptidoglycan (PG) remodeling and envelope constriction. Curvature of FtsZ filaments promotes membrane deformation in vitro, but its role in division in vivo remains undefined. Inside cells, FtsZ directs PG insertion at the division plane, though it is unclear how FtsZ structure and dynamics are mechanistically coupled to PG metabolism. Here we study FzlA, a division protein that stabilizes highly curved FtsZ filaments, as a tool for assessing the contribution of FtsZ filament curvature to constriction. We show that in Caulobacter crescentus, FzlA must bind to FtsZ for division to occur and that FzlA-mediated FtsZ curvature is correlated with efficient division. We observed that FzlA influences constriction rate, and that this activity is associated with its ability to bind and curve FtsZ polymers. Further, we found that a slowly constricting fzlA mutant strain develops 'pointy' poles, suggesting that FzlA influences the relative contributions of radial versus longitudinal PG insertion at the septum. These findings implicate FzlA as a critical coordinator of envelope constriction through its interaction with FtsZ and suggest a functional link between FtsZ curvature and efficient constriction in C. crescentus.

Indexed as

Bacterial ProteinsCaulobacter crescentusCell Cycle ProteinsCell DivisionCell MembraneCell WallCytoskeletal ProteinsGene LibraryGTP PhosphohydrolasesPeptidoglycanProtein BindingProtein Conformation, beta-StrandProtein Interaction Domains and MotifsBacterial ProteinsCell Cycle ProteinsCytoskeletal ProteinsFtsA protein, BacteriaFtsZ protein, BacteriaGTP PhosphohydrolasesPeptidoglycan

Identifiers

PMID29119622
PMCPMC5760450
OpenAlexW2767863220

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.