Evidence map›Paper›PMID 27028265›Full record

ArticleMolecular microbiology2016

A novel membrane anchor for FtsZ is linked to cell wall hydrolysis in Caulobacter crescentus.

Elizabeth L Meier, Shiva Razavi, Takanari Inoue, Erin D Goley

Abstract read
In one paragraph

Article in Molecular microbiology, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.

0numbers the graph read from it
0cells of the map it votes in
19citing papers in PubMed
–field-weighted citation impact
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

19 citing papers in PubMed.

  1. Article
  2. GTPase activity regulates FtsZ ring positioning inMolecular biology of the cell · 2024
    Article
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  4. Review
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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

4 authors.

Elizabeth L MeierDepartment of Biological Chemistry, Johns Hopkins University School of Medicine, 725 N. Wolfe Street, Baltimore, Maryland, 21205, USA.
Shiva RazaviDepartment of Biomedical Engineering, Johns Hopkins University School of Medicine, 720 Rutland Avenue, Baltimore, Maryland, 21205, USA.
Takanari InoueDepartment of Biomedical Engineering, Johns Hopkins University School of Medicine, 720 Rutland Avenue, Baltimore, Maryland, 21205, USA.
Erin D GoleyDepartment of Biological Chemistry, Johns Hopkins University School of Medicine, 725 N. Wolfe Street, Baltimore, Maryland, 21205, USA.ORCID 0000-0002-8518-2303

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
Feedback and Crosstalk in Eukaryotic Chemotaxis- Administrative SupplementR01GM092930 · NIGMS · JOHNS HOPKINS UNIVERSITY · PI INOUE, TAKANARI · 2010 to 2015
$1.6M
NIGMS NIH HHS R01 GM092930NIGMS NIH HHS R01 GM108640NIGMS NIH HHS T32 GM007445
6 · The paper itself

Abstract

In most bacteria, the tubulin-like GTPase FtsZ forms an annulus at midcell (the Z-ring) which recruits the division machinery and regulates cell wall remodeling. Although both activities require membrane attachment of FtsZ, few membrane anchors have been characterized. FtsA is considered to be the primary membrane tether for FtsZ in bacteria, however in Caulobacter crescentus, FtsA arrives at midcell after stable Z-ring assembly and early FtsZ-directed cell wall synthesis. We hypothesized that additional proteins tether FtsZ to the membrane and demonstrate that in C. crescentus, FzlC is one such membrane anchor. FzlC associates with membranes directly in vivo and in vitro and recruits FtsZ to membranes in vitro. As for most known membrane anchors, the C-terminal peptide of FtsZ is required for its recruitment to membranes by FzlC in vitro and midcell recruitment of FzlC in cells. In vivo, overproduction of FzlC causes cytokinesis defects whereas deletion of fzlC causes synthetic defects with dipM, ftsE and amiC mutants, implicating FzlC in cell wall hydrolysis. Our characterization of FzlC as a novel membrane anchor for FtsZ expands our understanding of FtsZ regulators and establishes a role for membrane-anchored FtsZ in the regulation of cell wall hydrolysis.

Indexed as

Bacterial ProteinsCaulobacter crescentusCell DivisionCell WallCytokinesisCytoskeletal ProteinsGTP PhosphohydrolasesHydrolysisMembrane ProteinsProtein BindingBacterial ProteinsCytoskeletal ProteinsFtsZ protein, BacteriaGTP PhosphohydrolasesMembrane Proteins

Identifiers

PMID27028265
PMCPMC4935632

What OpenQuestion holds

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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.