Evidence map›Paper›PMID 31317204›Full record

ReviewCellular and molecular life sciences : CMLS2019

The E. coli MinCDE system in the regulation of protein patterns and gradients.

Beatrice Ramm, Tamara Heermann, Petra Schwille

Abstract readReview
In one paragraph

Review in Cellular and molecular life sciences : CMLS, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 54 papers.

0numbers the graph read from it
0cells of the map it votes in
54citing 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

54 citing papers in PubMed.

  1. Review
  2. Article
  3. Devising a divisome for synthetic cells.Nature reviews. Chemistry · 2026
    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

3 authors.

Beatrice RammMax Planck Institute of Biochemistry, Am Klopferspitz 18, 82152, Martinsried, Germany.
Tamara HeermannMax Planck Institute of Biochemistry, Am Klopferspitz 18, 82152, Martinsried, Germany.
Petra SchwilleMax Planck Institute of Biochemistry, Am Klopferspitz 18, 82152, Martinsried, Germany. schwille@biochem.mpg.de.ORCID http://orcid.org/0000-0002-6106-4847

Funding

BMBF MaxSynBioDFG QBMDFG SFB1032DFG TRR174
6 · The paper itself

Abstract

Molecular self-organziation, also regarded as pattern formation, is crucial for the correct distribution of cellular content. The processes leading to spatiotemporal patterns often involve a multitude of molecules interacting in complex networks, so that only very few cellular pattern-forming systems can be regarded as well understood. Due to its compositional simplicity, the Escherichia coli MinCDE system has, thus, become a paradigm for protein pattern formation. This biological reaction diffusion system spatiotemporally positions the division machinery in E. coli and is closely related to ParA-type ATPases involved in most aspects of spatiotemporal organization in bacteria. The ATPase MinD and the ATPase-activating protein MinE self-organize on the membrane as a reaction matrix. In vivo, these two proteins typically oscillate from pole-to-pole, while in vitro they can form a variety of distinct patterns. MinC is a passenger protein supposedly operating as a downstream cue of the system, coupling it to the division machinery. The MinCDE system has helped to extract not only the principles underlying intracellular patterns, but also how they are shaped by cellular boundaries. Moreover, it serves as a model to investigate how patterns can confer information through specific and non-specific interactions with other molecules. Here, we review how the three Min proteins self-organize to form patterns, their response to geometric boundaries, and how these patterns can in turn induce patterns of other molecules, focusing primarily on experimental approaches and developments.

Indexed as

Adenosine TriphosphatasesCell Cycle ProteinsCell DivisionCell MembraneCytoplasmCytoskeletal ProteinsEscherichia coliEscherichia coli ProteinsMembrane ProteinsProtein MultimerizationProtein TransportAdenosine TriphosphatasesCell Cycle ProteinsCytoskeletal ProteinsEscherichia coli ProteinsMembrane ProteinsMinC protein, E coliMinD protein, E coliMinE protein, E coliFtsZGeometry sensingParA-type ATPaseReaction–diffusion mechanismReconstitutionSpatiotemporal regulation

Identifiers

PMID31317204
PMCPMC6803595

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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.