Evidence map›Paper›PMID 31848350›Full record

ArticleNature communications2019

Cooperative ordering of treadmilling filaments in cytoskeletal networks of FtsZ and its crosslinker ZapA.

Paulo Caldas, Mar López-Pelegrín, Daniel J G Pearce, Nazmi Burak Budanur, Jan Brugués, Martin Loose

Open access · goldAbstract read
In one paragraph

Article in Nature communications, 2019. 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
4.8field-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, 75 citations in OpenAlex.

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  14. The Division Defect of aJournal of bacteriology · 2021
    Article
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  20. FtsZ dynamics in bacterial division: What, how, and why?Current opinion in cell biology · 2021
    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

6 authors at 3 institutions in 3 countries.

Paulo CaldasInstitute of Science and Technology Austria, 3400, Klosterneuburg, Austria.ORCID http://orcid.org/0000-0001-6730-4461
Mar López-PelegrínInstitute of Science and Technology Austria, 3400, Klosterneuburg, Austria.
Daniel J G PearceSchool of Chemistry and Biochemistry, University of Geneva, 1211, Geneva, Switzerland.
Nazmi Burak BudanurInstitute of Science and Technology Austria, 3400, Klosterneuburg, Austria.
Jan BruguésMax Planck Institute of Molecular Cell Biology and Genetics, 01307, Dresden, Germany.ORCID http://orcid.org/0000-0002-6731-4130
Martin LooseInstitute of Science and Technology Austria, 3400, Klosterneuburg, Austria. martin.loose@ist.ac.at.
Institute of Science and Technology Austria · ATMax Planck Institute for the Physics of Complex Systems · DEUniversity of Geneva · CH

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

During bacterial cell division, the tubulin-homolog FtsZ forms a ring-like structure at the center of the cell. This Z-ring not only organizes the division machinery, but treadmilling of FtsZ filaments was also found to play a key role in distributing proteins at the division site. What regulates the architecture, dynamics and stability of the Z-ring is currently unknown, but FtsZ-associated proteins are known to play an important role. Here, using an in vitro reconstitution approach, we studied how the well-conserved protein ZapA affects FtsZ treadmilling and filament organization into large-scale patterns. Using high-resolution fluorescence microscopy and quantitative image analysis, we found that ZapA cooperatively increases the spatial order of the filament network, but binds only transiently to FtsZ filaments and has no effect on filament length and treadmilling velocity. Together, our data provides a model for how FtsZ-associated proteins can increase the precision and stability of the bacterial cell division machinery in a switch-like manner.

Indexed as

Bacterial ProteinsCarrier ProteinsCytokinesisCytoskeletal ProteinsCytoskeletonEscherichia coliEscherichia coli ProteinsImage Processing, Computer-AssistedIntravital MicroscopyMicroscopy, FluorescenceSingle Molecule ImagingBacterial ProteinsCarrier ProteinsCytoskeletal ProteinsEscherichia coli ProteinsFtsZ protein, BacteriaZapA protein, E coli

Identifiers

PMID31848350
PMCPMC6917738
OpenAlexW2996451414

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.