Evidence map›Paper›PMID 26739566›Full record

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

Geometry-induced protein pattern formation.

Dominik Thalmeier, Jacob Halatek, Erwin Frey

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 22 papers.

0numbers the graph read from it
0cells of the map it votes in
22citing papers in PubMed
9.9field-weighted citation impact, top 2% 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

22 citing papers in PubMed, 64 citations in OpenAlex.

  1. Signal control during tissue regeneration in adult animals.Nature reviews. Molecular cell biology · 2026
    Review
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  6. Turing Patterning in Stratified Domains.Bulletin of mathematical biology · 2020
    Article
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  13. Self-organization principles of intracellular pattern formation.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2018
    Review
  14. MinE conformational switching confers robustness on self-organized Min protein patterns.Proceedings of the National Academy of Sciences of the United States of America · 2018
    Article
  15. Article
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  17. Review
  18. Systems biology of cellular membranes: a convergence with biophysics.Wiley interdisciplinary reviews. Systems biology and medicine · 2017
    Review
  19. 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 at 2 institutions in 2 countries.

Dominik ThalmeierArnold Sommerfeld Center for Theoretical Physics, Ludwig-Maximilians-Universität München, D-80333 Munich, Germany; Center for NanoScience, Ludwig-Maximilians-Universität München, D-80333 Munich, Germany; Donders Institute, Radboud University, 6525 EZ Nijmegen, The Netherlands; Department of Biophysics, Radboud University, 6525 AJ Nijmegen, The Netherlands.
Jacob HalatekArnold Sommerfeld Center for Theoretical Physics, Ludwig-Maximilians-Universität München, D-80333 Munich, Germany; Center for NanoScience, Ludwig-Maximilians-Universität München, D-80333 Munich, Germany;
Erwin FreyArnold Sommerfeld Center for Theoretical Physics, Ludwig-Maximilians-Universität München, D-80333 Munich, Germany; Center for NanoScience, Ludwig-Maximilians-Universität München, D-80333 Munich, Germany; frey@lmu.de.
Center for NanoScience · DELudwig-Maximilians-Universität München · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Protein patterns are known to adapt to cell shape and serve as spatial templates that choreograph downstream processes like cell polarity or cell division. However, how can pattern-forming proteins sense and respond to the geometry of a cell, and what mechanistic principles underlie pattern formation? Current models invoke mechanisms based on dynamic instabilities arising from nonlinear interactions between proteins but neglect the influence of the spatial geometry itself. Here, we show that patterns can emerge as a direct result of adaptation to cell geometry, in the absence of dynamical instability. We present a generic reaction module that allows protein densities robustly to adapt to the symmetry of the spatial geometry. The key component is an NTPase protein that cycles between nucleotide-dependent membrane-bound and cytosolic states. For elongated cells, we find that the protein dynamics generically leads to a bipolar pattern, which vanishes as the geometry becomes spherically symmetrical. We show that such a reaction module facilitates universal adaptation to cell geometry by sensing the local ratio of membrane area to cytosolic volume. This sensing mechanism is controlled by the membrane affinities of the different states. We apply the theory to explain AtMinD bipolar patterns in [Formula: see text] EcMinDE Escherichia coli. Due to its generic nature, the mechanism could also serve as a hitherto-unrecognized spatial template in many other bacterial systems. Moreover, the robustness of the mechanism enables self-organized optimization of protein patterns by evolutionary processes. Finally, the proposed module can be used to establish geometry-sensitive protein gradients in synthetic biological systems.

Indexed as

Cell PolarityCytosolModels, BiologicalProtein ConformationProteinsProteinscell polaritygeometry sensingMin systemnonlinear dynamicspattern formation

Identifiers

PMID26739566
PMCPMC4725492
OpenAlexW2228631656

What OpenQuestion holds

Textmetadata
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.