ArticleProceedings of the National Academy of Sciences of the United States of America2018
MinE conformational switching confers robustness on self-organized Min protein patterns.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 32 papers.
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.
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.
Who cites it
32 citing papers in PubMed, 84 citations in OpenAlex.
- Fold-Switching Proteins.Annual review of biophysics · 2026Review
- Cell-Size Confinement Drives Size-Dependent Scaling of Intracellular Reaction-Diffusion Waves for Robust Patterning.Small science · 2026Article
- 3D pattern formation of a protein-membrane suspension.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Protein dimerization in 2D vs 3D: Geometric allostery enhances binding affinity.The Journal of chemical physics · 2025Article
- Fold-switching proteins.ArXiv · 2025Article
- Growth-dependent concentration gradient of the oscillating Min system in Escherichia coli.The Journal of cell biology · 2025Article
- Robust and resource-optimal dynamic pattern formation of Min proteins in vivo.Nature physics · 2025Article
- Addendum: Directing Min protein patterns with advective bulk flow.Nature communications · 2024Article
- Forceful patterning: theoretical principles of mechanochemical pattern formation.EMBO reports · 2023Review
- The mechanism of MinD stability modulation by MinE in Min protein dynamics.PLoS computational biology · 2023Article
- Directing Min protein patterns with advective bulk flow.Nature communications · 2023Article
- Bridging scales in a multiscale pattern-forming system.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- Dissecting cell fate dynamics in pediatric glioblastoma through the lens of complex systems and cellular cybernetics.Biological cybernetics · 2022Review
- Mode selection mechanism in traveling and standing waves revealed by Min wave reconstituted in artificial cells.Science advances · 2022Article
- How Do MinC-D Copolymers Act on Z-Ring Localization Regulation? A New Model ofFrontiers in microbiology · 2022Article
- A Review of Mathematical and Computational Methods in Cancer Dynamics.Frontiers in oncology · 2022Review
- Increasing MinD's Membrane Affinity Yields Standing Wave Oscillations and Functional Gradients on Flat Membranes.ACS synthetic biology · 2021Article
- Speed limits of protein assembly with reversible membrane localization.The Journal of chemical physics · 2021Article
- Article
- A review of dynamical systems approaches for the detection of chaotic attractors in cancer networks.Patterns (New York, N.Y.) · 2021Review
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
6 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Protein patterning is vital for many fundamental cellular processes. This raises two intriguing questions: Can such intrinsically complex processes be reduced to certain core principles and, if so, what roles do the molecular details play in individual systems? A prototypical example for protein patterning is the bacterial Min system, in which self-organized pole-to-pole oscillations of MinCDE proteins guide the cell division machinery to midcell. These oscillations are based on cycling of the ATPase MinD and its activating protein MinE between the membrane and the cytoplasm. Recent biochemical evidence suggests that MinE undergoes a reversible, MinD-dependent conformational switch from a latent to a reactive state. However, the functional relevance of this switch for the Min network and pattern formation remains unclear. By combining mathematical modeling and in vitro reconstitution of mutant proteins, we dissect the two aspects of MinE's switch, persistent membrane binding and a change in MinE's affinity for MinD. Our study shows that the MinD-dependent change in MinE's binding affinity for MinD is essential for patterns to emerge over a broad and physiological range of protein concentrations. Mechanistically, our results suggest that conformational switching of an ATPase-activating protein can lead to the spatial separation of its distinct functional states and thereby confer robustness on an intracellular protein network with vital roles in bacterial cell division.
Indexed as
Identifiers
What OpenQuestion holds
Registered trials
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.