Evidence map›Paper›PMID 26884160›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2016

Membrane-bound MinDE complex acts as a toggle switch that drives Min oscillation coupled to cytoplasmic depletion of MinD.

Anthony G Vecchiarelli, Min Li, Michiyo Mizuuchi, Ling Chin Hwang, Yeonee Seol, Keir C Neuman, Kiyoshi Mizuuchi

Abstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 59 papers.

0numbers the graph read from it
0cells of the map it votes in
59citing 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

59 citing papers in PubMed.

  1. Article
  2. Article
  3. Review
  4. Article
  5. Article
  6. Frontiers in cell and developmental biology · 2025
    Review
  7. Article
  8. Article
  9. Review
  10. Article
  11. Impact of Negative Feedbacks on De Novo Pyrimidines Biosynthesis inInternational journal of molecular sciences · 2023
    Article
  12. Article
  13. Article
  14. Bridging scales in a multiscale pattern-forming system.Proceedings of the National Academy of Sciences of the United States of America · 2022
    Article
  15. Article
  16. Article
  17. Article
  18. Review
  19. Article
  20. CTP andeLife · 2021
    Article
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

7 authors.

Anthony G VecchiarelliLaboratory of Molecular Biology, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, MD 20892;
Min LiLaboratory of Molecular Biology, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, MD 20892;
Michiyo MizuuchiLaboratory of Molecular Biology, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, MD 20892;
Ling Chin HwangLaboratory of Molecular Biology, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, MD 20892;
Yeonee SeolLaboratory of Single Molecule Biophysics, National Heart, Lung, and Blood Institute, National Institutes of Health, Bethesda, MD 20892.
Keir C NeumanLaboratory of Single Molecule Biophysics, National Heart, Lung, and Blood Institute, National Institutes of Health, Bethesda, MD 20892.
Kiyoshi MizuuchiLaboratory of Molecular Biology, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, MD 20892; kiyoshimi@helix.nih.gov.

Funding

Single-molecule measurements of DNA topology and topoisomerasesZIAHL001056 · NHLBI · NATIONAL HEART, LUNG, AND BLOOD INSTITUTE · PI NEUMAN, KEIR · 2009 to 2025
$22.6M
Study of the mechanism of septum localization during bacterial cell divisionZIADK036164 · NIDDK · NATIONAL INSTITUTE OF DIABETES AND DIGESTIVE AND KIDNEY DISEASES · PI MIZUUCHI, KIYOSHI · 2009 to 2025
$12.7M
Single-molecule measurements of collagen processing by Matrix MetalloproteinasesZIAHL006114 · NHLBI · NATIONAL HEART, LUNG, AND BLOOD INSTITUTE · PI NEUMAN, KEIR · 2011 to 2017
$1.1M
Intramural NIH HHS
6 · The paper itself

Abstract

The Escherichia coli Min system self-organizes into a cell-pole to cell-pole oscillator on the membrane to prevent divisions at the cell poles. Reconstituting the Min system on a lipid bilayer has contributed to elucidating the oscillatory mechanism. However, previous in vitro patterns were attained with protein densities on the bilayer far in excess of those in vivo and failed to recapitulate the standing wave oscillations observed in vivo. Here we studied Min protein patterning at limiting MinD concentrations reflecting the in vivo conditions. We identified "burst" patterns--radially expanding and imploding binding zones of MinD, accompanied by a peripheral ring of MinE. Bursts share several features with the in vivo dynamics of the Min system including standing wave oscillations. Our data support a patterning mechanism whereby the MinD-to-MinE ratio on the membrane acts as a toggle switch: recruiting and stabilizing MinD on the membrane when the ratio is high and releasing MinD from the membrane when the ratio is low. Coupling this toggle switch behavior with MinD depletion from the cytoplasm drives a self-organized standing wave oscillator.

Indexed as

Adenosine TriphosphatasesCell Cycle ProteinsCell-Free SystemCell MembraneCytoplasmEscherichia coli ProteinsGreen Fluorescent ProteinsImage Processing, Computer-AssistedLipid BilayersMicroscopy, FluorescenceProtein MultimerizationAdenosine TriphosphatasesCell Cycle ProteinsEscherichia coli ProteinsGreen Fluorescent ProteinsLipid BilayersMinD protein, E coliMinE protein, E colicell divisionintracellular positioningpattern formationself-organizationsubcellular organization

Identifiers

PMID26884160
PMCPMC4801307

What OpenQuestion holds

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Registered trials

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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.