Evidence map›Paper›PMID 34521846›Full record

ArticleNature communications2021

Mechanosensitive recruitment of stator units promotes binding of the response regulator CheY-P to the flagellar motor.

Jyot D Antani, Rachit Gupta, Annie H Lee, Kathy Y Rhee, Michael D Manson, Pushkar P Lele

Abstract read
In one paragraph

Article in Nature communications, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.

0numbers the graph read from it
0cells of the map it votes in
25citing 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

25 citing papers in PubMed.

  1. Review
  2. Review
  3. The dynamic response of the bacterial flagellar motor to its direct intracellular input signal.Proceedings of the National Academy of Sciences of the United States of America · 2026
    Article
  4. Article
  5. Article
  6. Review
  7. Microscopic phage adsorption assay: High-throughput quantification of virus particle attachment to host bacterial cells.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  8. Review
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Article
  20. FliL ring enhances the function of periplasmic flagella.Proceedings of the National Academy of Sciences of the United States of America · 2022
    Article
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

6 authors.

Jyot D AntaniArtie McFerrin Department of Chemical Engineering, Texas A&M University, College Station, TX, 77843-3122, USA.ORCID 0000-0002-7402-983X
Rachit GuptaArtie McFerrin Department of Chemical Engineering, Texas A&M University, College Station, TX, 77843-3122, USA.ORCID 0000-0003-4681-6374
Annie H LeeArtie McFerrin Department of Chemical Engineering, Texas A&M University, College Station, TX, 77843-3122, USA.ORCID 0000-0001-9183-3021
Kathy Y RheeArtie McFerrin Department of Chemical Engineering, Texas A&M University, College Station, TX, 77843-3122, USA.
Michael D MansonDepartment of Biology, Texas A&M University, College Station, TX, 77843-3258, USA.
Pushkar P LeleArtie McFerrin Department of Chemical Engineering, Texas A&M University, College Station, TX, 77843-3122, USA. plele@tamu.edu.ORCID 0000-0002-2894-3487

Funding

Mechanical Regulation of Ultra-Sensitivity in E. Coli Flagellar MotorsR01GM123085 · NIGMS · TEXAS ENGINEERING EXPERIMENT STATION · PI LELE, PUSHKAR PRAKASH · 2017 to 2025
$1.8M
NIGMS NIH HHS R01 GM123085
6 · The paper itself

Abstract

Reversible switching of the bacterial flagellar motor between clockwise (CW) and counterclockwise (CCW) rotation is necessary for chemotaxis, which enables cells to swim towards favorable chemical habitats. Increase in the viscous resistance to the rotation of the motor (mechanical load) inhibits switching. However, cells must maintain homeostasis in switching to navigate within environments of different viscosities. The mechanism by which the cell maintains optimal chemotactic function under varying loads is not understood. Here, we show that the flagellar motor allosterically controls the binding affinity of the chemotaxis response regulator, CheY-P, to the flagellar switch complex by modulating the mechanical forces acting on the rotor. Mechanosensitive CheY-P binding compensates for the load-induced loss of switching by precisely adapting the switch response to a mechanical stimulus. The interplay between mechanical forces and CheY-P binding tunes the chemotactic function to match the load. This adaptive response of the chemotaxis output to mechanical stimuli resembles the proprioceptive feedback in the neuromuscular systems of insects and vertebrates.

Indexed as

Allosteric RegulationAnimalsBacterial ProteinsBiological MimicryBiomechanical PhenomenaChemotaxisEscherichia coliEscherichia coli ProteinsFeedback, SensoryFlagellaGene ExpressionInsectaMethyl-Accepting Chemotaxis ProteinsOptical TweezersProtein BindingVertebratesBacterial ProteinscheY protein, E coliEscherichia coli ProteinsFlig protein, BacteriaFliM protein, BacteriaFliN protein, BacteriaMethyl-Accepting Chemotaxis ProteinsMotA protein, BacteriaMotB protein, Bacteria

Identifiers

PMID34521846
PMCPMC8440544

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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.