Evidence map›Paper›PMID 29183968›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2017

Catch bond drives stator mechanosensitivity in the bacterial flagellar motor.

Ashley L Nord, Emilie Gachon, Ruben Perez-Carrasco, Jasmine A Nirody, Alessandro Barducci, Richard M Berry, Francesco Pedaci

Abstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 70 papers.

0numbers the graph read from it
0cells of the map it votes in
70citing 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

70 citing papers in PubMed.

  1. Journal of bacteriology · 2026
    Review
  2. TheProceedings of the National Academy of Sciences of the United States of America · 2026
    Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Torque-generating units of the bacterial flagellar motor are rotary motors.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  8. Article
  9. Article
  10. Osmotic stress triggers fast and reversible PMF collapse inbioRxiv : the preprint server for biology · 2025
    Article
  11. Article
  12. Article
  13. Review
  14. Article
  15. Article
  16. Measuring Bacterial Flagellar Motor Dynamics via a Bead Assay.Methods in molecular biology (Clifton, N.J.) · 2025
    Article
  17. Article
  18. Review
  19. Article
  20. Review

10 more citing papers are in PubMed but not listed here.

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.

Ashley L NordCentre de Biochimie Structurale (CBS), INSERM, CNRS, Université de Montpellier, 34090 Montpellier, France.
Emilie GachonCentre de Biochimie Structurale (CBS), INSERM, CNRS, Université de Montpellier, 34090 Montpellier, France.
Ruben Perez-CarrascoDepartment of Mathematics, University College London, London WC1E 6BT, United Kingdom.ORCID 0000-0001-5348-8829
Jasmine A NirodyBiophysics Graduate Group, University of California, Berkeley, CA 94720.
Alessandro BarducciCentre de Biochimie Structurale (CBS), INSERM, CNRS, Université de Montpellier, 34090 Montpellier, France.ORCID 0000-0002-1911-8039
Richard M BerryDepartment of Physics, Clarendon Laboratory, University of Oxford, Oxford OX1 2JD, United Kingdom.
Francesco PedaciCentre de Biochimie Structurale (CBS), INSERM, CNRS, Université de Montpellier, 34090 Montpellier, France; francesco.pedaci@cbs.cnrs.fr.ORCID 0000-0002-4530-3027

Funding

Biotechnology and Biological Sciences Research Council BB/E00458X/1Biotechnology and Biological Sciences Research Council BB/H01991X/1Wellcome TrustWellcome Trust WT098325MA
6 · The paper itself

Abstract

The bacterial flagellar motor (BFM) is the rotary motor that rotates each bacterial flagellum, powering the swimming and swarming of many motile bacteria. The torque is provided by stator units, ion motive force-powered ion channels known to assemble and disassemble dynamically in the BFM. This turnover is mechanosensitive, with the number of engaged units dependent on the viscous load experienced by the motor through the flagellum. However, the molecular mechanism driving BFM mechanosensitivity is unknown. Here, we directly measure the kinetics of arrival and departure of the stator units in individual motors via analysis of high-resolution recordings of motor speed, while dynamically varying the load on the motor via external magnetic torque. The kinetic rates obtained, robust with respect to the details of the applied adsorption model, indicate that the lifetime of an assembled stator unit increases when a higher force is applied to its anchoring point in the cell wall. This provides strong evidence that a catch bond (a bond strengthened instead of weakened by force) drives mechanosensitivity of the flagellar motor complex. These results add the BFM to a short, but growing, list of systems demonstrating catch bonds, suggesting that this "molecular strategy" is a widespread mechanism to sense and respond to mechanical stress. We propose that force-enhanced stator adhesion allows the cell to adapt to a heterogeneous environmental viscosity and may ultimately play a role in surface-sensing during swarming and biofilm formation.

Indexed as

Biomechanical PhenomenaEscherichia coliEscherichia coli ProteinsFlagellaKineticsModels, MolecularMolecular Motor ProteinsEscherichia coli ProteinsMolecular Motor Proteinsbacterial flagellar motorcatch bondEscherichia colimechanosensitivitymolecular motor

Identifiers

PMID29183968
PMCPMC5724282

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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.