Evidence map›Paper›PMID 27725777›Full record

ArticleScientific reports2016

Microenvironments created by liquid-liquid phase transition control the dynamic distribution of bacterial division FtsZ protein.

Begoña Monterroso, Silvia Zorrilla, Marta Sobrinos-Sanguino, Christine D Keating, Germán Rivas

Abstract read
In one paragraph

Article in Scientific reports, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.

0numbers the graph read from it
0cells of the map it votes in
27citing 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

27 citing papers in PubMed.

  1. Review
  2. 'Intelligent' proteins.Cellular and molecular life sciences : CMLS · 2025
    Review
  3. Article
  4. Article
  5. Review
  6. Article
  7. Bacterial lipid biophysics and membrane organization.Current opinion in microbiology · 2023
    Review
  8. Article
  9. Article
  10. Review
  11. Article
  12. Article
  13. Review
  14. Review
  15. Article
  16. Review
  17. 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

5 authors.

Begoña MonterrosoCentro de Investigaciones Biológicas, Consejo Superior de Investigaciones Científicas (CSIC), 28040, Madrid, Spain.
Silvia ZorrillaCentro de Investigaciones Biológicas, Consejo Superior de Investigaciones Científicas (CSIC), 28040, Madrid, Spain.
Marta Sobrinos-SanguinoCentro de Investigaciones Biológicas, Consejo Superior de Investigaciones Científicas (CSIC), 28040, Madrid, Spain.
Christine D KeatingDepartment of Chemistry, Pennsylvania State University, University Park, Pennsylvania 16802, USA.
Germán RivasCentro de Investigaciones Biológicas, Consejo Superior de Investigaciones Científicas (CSIC), 28040, Madrid, Spain.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The influence of membrane-free microcompartments resulting from crowding-induced liquid/liquid phase separation (LLPS) on the dynamic spatial organization of FtsZ, the main component of the bacterial division machinery, has been studied using several LLPS systems. The GTP-dependent assembly cycle of FtsZ is thought to be crucial for the formation of the septal ring, which is highly regulated in time and space. We found that FtsZ accumulates in one of the phases and/or at the interface, depending on the system composition and on the oligomerization state of the protein. These results were observed both in bulk LLPS and in lipid-stabilized, phase-separated aqueous microdroplets. The visualization of the droplets revealed that both the location and structural arrangement of FtsZ filaments is determined by the nature of the LLPS. Relocation upon depolymerization of the dynamic filaments suggests the protein may shift among microenvironments in response to changes in its association state. The existence of these dynamic compartments driven by phase transitions can alter the local composition and reactivity of FtsZ during its life cycle acting as a nonspecific modulating factor of cell function.

Indexed as

Phase TransitionBacterial ProteinsCytoplasmCytoskeletal ProteinsEscherichia coliGuanosine TriphosphateProtein MultimerizationBacterial ProteinsCytoskeletal ProteinsFtsZ protein, BacteriaGuanosine Triphosphate

Identifiers

PMID27725777
PMCPMC5057132

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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.