Evidence map›Paper›PMID 38781330›Full record

ArticleScience advances2024

Spatiotemporal dynamics of the proton motive force on single bacterial cells.

Anaïs Biquet-Bisquert, Baptiste Carrio, Nathan Meyer, Thales F D Fernandes, Manouk Abkarian, Farida Seduk, Axel Magalon, Ashley L Nord, Francesco Pedaci

Abstract read
In one paragraph

Article in Science advances, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.

0numbers the graph read from it
0cells of the map it votes in
15citing 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

15 citing papers in PubMed.

  1. Article
  2. Article
  3. Article
  4. ATP synthase activity boosts membrane proton acceptance and lateral diffusion.Proceedings of the National Academy of Sciences of the United States of America · 2026
    Article
  5. Article
  6. Article
  7. Review
  8. Review
  9. Osmotic stress triggers fast and reversible PMF collapse inbioRxiv : the preprint server for biology · 2025
    Article
  10. Article
  11. Review
  12. Review
  13. Article
  14. Article
  15. 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

9 authors.

Anaïs Biquet-BisquertCentre de Biologie Structurale, Université de Montpellier, CNRS, INSERM. Montpellier, France.ORCID 0000-0002-9314-1296
Baptiste CarrioCentre de Biologie Structurale, Université de Montpellier, CNRS, INSERM. Montpellier, France.
Nathan MeyerCentre de Biologie Structurale, Université de Montpellier, CNRS, INSERM. Montpellier, France.
Thales F D FernandesCentre de Biologie Structurale, Université de Montpellier, CNRS, INSERM. Montpellier, France.ORCID 0000-0003-3868-9029
Manouk AbkarianCentre de Biologie Structurale, Université de Montpellier, CNRS, INSERM. Montpellier, France.ORCID 0000-0003-0411-3187
Farida SedukAix Marseille Université, CNRS, Laboratoire de Chimie Bactérienne (UMR7283), IMM, IM2B, 13402 Marseille, France.
Axel MagalonAix Marseille Université, CNRS, Laboratoire de Chimie Bactérienne (UMR7283), IMM, IM2B, 13402 Marseille, France.ORCID 0000-0002-3375-738X
Ashley L NordCentre de Biologie Structurale, Université de Montpellier, CNRS, INSERM. Montpellier, France.ORCID 0000-0001-6199-2769
Francesco PedaciCentre de Biologie Structurale, Université de Montpellier, CNRS, INSERM. Montpellier, France.ORCID 0000-0002-4530-3027

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Electrochemical gradients across biological membranes are vital for cellular bioenergetics. In bacteria, the proton motive force (PMF) drives essential processes like adenosine triphosphate production and motility. Traditionally viewed as temporally and spatially stable, recent research reveals a dynamic PMF behavior at both single-cell and community levels. Moreover, the observed lateral segregation of respiratory complexes could suggest a spatial heterogeneity of the PMF. Using a light-activated proton pump and detecting the activity of the bacterial flagellar motor, we perturb and probe the PMF of single cells. Spatially homogeneous PMF perturbations reveal millisecond-scale temporal dynamics and an asymmetrical capacitive response. Localized perturbations show a rapid lateral PMF homogenization, faster than proton diffusion, akin to the electrotonic potential spread observed in passive neurons, explained by cable theory. These observations imply a global coupling between PMF sources and consumers along the membrane, precluding sustained PMF spatial heterogeneity but allowing for rapid temporal changes.

Indexed as

Proton-Motive ForceAdenosine TriphosphateBacteriaFlagellaProtonsSingle-Cell AnalysisSpatio-Temporal AnalysisAdenosine TriphosphateProtons

Identifiers

PMID38781330
PMCPMC11114223

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.