Evidence map›Paper›PMID 35789161›Full record

ArticleNature communications2022

Elasticity of podosome actin networks produces nanonewton protrusive forces.

Marion Jasnin, Jordan Hervy, Stéphanie Balor, Anaïs Bouissou, Amsha Proag, Raphaël Voituriez, Jonathan Schneider, Thomas Mangeat, Isabelle Maridonneau-Parini, Wolfgang Baumeister and 2 more

Open access · goldAbstract read
In one paragraph

Article in Nature communications, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.

0numbers the graph read from it
0cells of the map it votes in
18citing papers in PubMed
3.6field-weighted citation impact, top 6% of its field
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

18 citing papers in PubMed, 32 citations in OpenAlex.

  1. Article
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  4. Podosomes and Mechanical Force.Results and problems in cell differentiation · 2026
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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

12 authors at 2 institutions in 2 countries.

Marion JasninDepartment of Molecular Structural Biology, Max Planck Institute of Biochemistry, Martinsried, Germany. jasnin@biochem.mpg.de.ORCID 0000-0003-1726-4566
Jordan HervyUniversité de Paris, CNRS, Institut Jacques Monod, Paris, France.
Stéphanie BalorPlateforme de Microscopie Électronique Intégrative, Centre de Biologie Intégrative, CNRS, UPS, Toulouse, France.
Anaïs BouissouInstitut de Pharmacologie et de Biologie Structurale, Université de Toulouse, CNRS, UPS, Toulouse, France.
Amsha ProagInstitut de Pharmacologie et de Biologie Structurale, Université de Toulouse, CNRS, UPS, Toulouse, France.ORCID 0000-0003-3366-7365
Raphaël VoituriezLaboratoire Jean Perrin, CNRS, Sorbonne Université, Paris, France.ORCID 0000-0001-8746-5713
Jonathan SchneiderDepartment of Molecular Structural Biology, Max Planck Institute of Biochemistry, Martinsried, Germany.
Thomas MangeatLITC Core Facility, Centre de Biologie Integrative, Université de Toulouse, CNRS, UPS, 31062, Toulouse, France.
Isabelle Maridonneau-PariniInstitut de Pharmacologie et de Biologie Structurale, Université de Toulouse, CNRS, UPS, Toulouse, France.
Wolfgang BaumeisterDepartment of Molecular Structural Biology, Max Planck Institute of Biochemistry, Martinsried, Germany.ORCID 0000-0001-8154-8809
Serge DmitrieffUniversité de Paris, CNRS, Institut Jacques Monod, Paris, France. serge.dmitrieff@ijm.fr.ORCID 0000-0002-1362-5670
Renaud PoinclouxInstitut de Pharmacologie et de Biologie Structurale, Université de Toulouse, CNRS, UPS, Toulouse, France. renaud.poincloux@ipbs.fr.ORCID 0000-0003-2884-1744
Centre National de la Recherche Scientifique · FRMax Planck Institute of Biochemistry · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Actin filaments assemble into force-generating systems involved in diverse cellular functions, including cell motility, adhesion, contractility and division. It remains unclear how networks of actin filaments, which individually generate piconewton forces, can produce forces reaching tens of nanonewtons. Here we use in situ cryo-electron tomography to unveil how the nanoscale architecture of macrophage podosomes enables basal membrane protrusion. We show that the sum of the actin polymerization forces at the membrane is not sufficient to explain podosome protrusive forces. Quantitative analysis of podosome organization demonstrates that the core is composed of a dense network of bent actin filaments storing elastic energy. Theoretical modelling of the network as a spring-loaded elastic material reveals that it exerts forces of a few tens of nanonewtons, in a range similar to that evaluated experimentally. Thus, taking into account not only the interface with the membrane but also the bulk of the network, is crucial to understand force generation by actin machineries. Our integrative approach sheds light on the elastic behavior of dense actin networks and opens new avenues to understand force production inside cells.

Indexed as

PodosomesActin CytoskeletonActinsCell MovementElasticityActins

Identifiers

PMID35789161
PMCPMC9253342
OpenAlexW4283793060

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.