Evidence map›Paper›PMID 30258191›Full record

ArticleNature communications2018

The MinDE system is a generic spatial cue for membrane protein distribution in vitro.

Beatrice Ramm, Philipp Glock, Jonas Mücksch, Philipp Blumhardt, Daniela A García-Soriano, Michael Heymann, Petra Schwille

Abstract read
In one paragraph

Article in Nature communications, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.

0numbers the graph read from it
0cells of the map it votes in
24citing 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

24 citing papers in PubMed.

  1. A conserved oscillatory system that positions the divisome in Archaea.bioRxiv : the preprint server for biology · 2026
    Article
  2. 3D pattern formation of a protein-membrane suspension.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
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  15. Towards a synthetic cell cycle.Nature communications · 2021
    Review
  16. Article
  17. Article
  18. Article
  19. Cooperatively enhanced reactivity and "stabilitaxis" of dissociating oligomeric proteins.Proceedings of the National Academy of Sciences of the United States of America · 2020
    Article
  20. 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

7 authors.

Beatrice RammMax Planck Institute of Biochemistry, Am Klopferspitz 18, 82152, Martinsried, Germany.ORCID http://orcid.org/0000-0002-7402-1942
Philipp GlockMax Planck Institute of Biochemistry, Am Klopferspitz 18, 82152, Martinsried, Germany.ORCID http://orcid.org/0000-0002-0238-2634
Jonas MückschMax Planck Institute of Biochemistry, Am Klopferspitz 18, 82152, Martinsried, Germany.ORCID http://orcid.org/0000-0002-1469-6956
Philipp BlumhardtMax Planck Institute of Biochemistry, Am Klopferspitz 18, 82152, Martinsried, Germany.ORCID http://orcid.org/0000-0001-5510-4809
Daniela A García-SorianoMax Planck Institute of Biochemistry, Am Klopferspitz 18, 82152, Martinsried, Germany.ORCID http://orcid.org/0000-0003-2849-8528
Michael HeymannMax Planck Institute of Biochemistry, Am Klopferspitz 18, 82152, Martinsried, Germany.ORCID http://orcid.org/0000-0002-9278-8207
Petra SchwilleMax Planck Institute of Biochemistry, Am Klopferspitz 18, 82152, Martinsried, Germany. schwille@biochem.mpg.de.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The E. coli MinCDE system has become a paradigmatic reaction-diffusion system in biology. The membrane-bound ATPase MinD and ATPase-activating protein MinE oscillate between the cell poles followed by MinC, thus positioning the main division protein FtsZ at midcell. Here we report that these energy-consuming MinDE oscillations may play a role beyond constraining MinC/FtsZ localization. Using an in vitro reconstitution assay, we show that MinDE self-organization can spatially regulate a variety of functionally completely unrelated membrane proteins into patterns and gradients. By concentration waves sweeping over the membrane, they induce a direct net transport of tightly membrane-attached molecules. That the MinDE system can spatiotemporally control a much larger set of proteins than previously known, may constitute a MinC-independent pathway to division site selection and chromosome segregation. Moreover, the here described phenomenon of active transport through a traveling diffusion barrier may point to a general mechanism of spatiotemporal regulation in cells.

Indexed as

Adenosine TriphosphatasesAdenosine TriphosphateBacterial ProteinsCell Cycle ProteinsCytoskeletal ProteinsDNAEscherichia coliEscherichia coli ProteinsMembrane ProteinsAdenosine TriphosphatasesAdenosine TriphosphateBacterial ProteinsCell Cycle ProteinsCytoskeletal ProteinsDNAEscherichia coli ProteinsFtsZ protein, BacteriaMembrane ProteinsMinD protein, E coliMinE protein, E coli

Identifiers

PMID30258191
PMCPMC6158289

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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.