Evidence map›Paper›PMID 38658549›Full record

ArticleNature communications2024

F-actin architecture determines the conversion of chemical energy into mechanical work.

Ryota Sakamoto, Michael P Murrell

Abstract read
In one paragraph

Article in Nature communications, 2024. 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. Article
  2. Article
  3. Article
  4. Article
  5. Energetic gradients emerge in developing motor-microtubule structures.bioRxiv : the preprint server for biology · 2026
    Article
  6. Article
  7. Article
  8. Article
  9. Review
  10. Article
  11. Review
  12. Review
  13. Review
  14. Article
  15. Review
  16. Clustered macrophages cooperate to eliminate tumors via coordinated intrudopodia.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  17. Ecosystems as adaptive living circuits.bioRxiv : the preprint server for biology · 2025
    Article
  18. Review
  19. Filament transport supports contractile steady states of actin networks.bioRxiv : the preprint server for biology · 2025
    Article
  20. 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

2 authors.

Ryota SakamotoDepartment of Biomedical Engineering, Yale University, 10 Hillhouse Avenue, New Haven, CT, USA.ORCID http://orcid.org/0000-0002-7762-3682
Michael P MurrellDepartment of Biomedical Engineering, Yale University, 10 Hillhouse Avenue, New Haven, CT, USA. michael.murrell@yale.edu.ORCID http://orcid.org/0000-0001-6788-2077

Funding

Systems analysis of phenotypic switch in control of cancer invasionU54CA209992 · NCI · YALE UNIVERSITY · PI LEVCHENKO, ANDRE · 2016 to 2021
$10.1M
Universal Roles of Force Generation and Transmission in Biological SystemsR01GM126256 · NIGMS · PURDUE UNIVERSITY · PI KIM, TAEYOON · 2017 to 2021
$2.3M
NCI NIH HHS U54 CA209992NIGMS NIH HHS R01 GM126256
6 · The paper itself

Abstract

Mechanical work serves as the foundation for dynamic cellular processes, ranging from cell division to migration. A fundamental driver of cellular mechanical work is the actin cytoskeleton, composed of filamentous actin (F-actin) and myosin motors, where force generation relies on adenosine triphosphate (ATP) hydrolysis. F-actin architectures, whether bundled by crosslinkers or branched via nucleators, have emerged as pivotal regulators of myosin II force generation. However, it remains unclear how distinct F-actin architectures impact the conversion of chemical energy to mechanical work. Here, we employ in vitro reconstitution of distinct F-actin architectures with purified components to investigate their influence on myosin ATP hydrolysis (consumption). We find that F-actin bundles composed of mixed polarity F-actin hinder network contraction compared to non-crosslinked network and dramatically decelerate ATP consumption rates. Conversely, linear-nucleated networks allow network contraction despite reducing ATP consumption rates. Surprisingly, branched-nucleated networks facilitate high ATP consumption without significant network contraction, suggesting that the branched network dissipates energy without performing work. This study establishes a link between F-actin architecture and myosin energy consumption, elucidating the energetic principles underlying F-actin structure formation and the performance of mechanical work.

Indexed as

ActinsAdenosine TriphosphateActin CytoskeletonAnimalsBiomechanical PhenomenaHydrolysisMyosinsMyosin Type IIRabbitsActinsAdenosine TriphosphateMyosinsMyosin Type II

Identifiers

PMID38658549
PMCPMC11043346

What OpenQuestion holds

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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.