Evidence map›Paper›PMID 24062578›Full record

ArticlePhilosophical transactions of the Royal Society of London. Series B, Biological sciences2013

Actin polymerization or myosin contraction: two ways to build up cortical tension for symmetry breaking.

Kevin Carvalho, Joël Lemière, Fahima Faqir, John Manzi, Laurent Blanchoin, Julie Plastino, Timo Betz, Cécile Sykes

Abstract read
In one paragraph

Article in Philosophical transactions of the Royal Society of London. Series B, Biological sciences, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 42 papers.

0numbers the graph read from it
0cells of the map it votes in
42citing 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

42 citing papers in PubMed.

  1. Article
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  7. Characterization of early and late events of adherens junction assembly.bioRxiv : the preprint server for biology · 2024
    Article
  8. Article
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  11. Methods to mechanically perturb and characterize GUV-based minimal cell models.Computational and structural biotechnology journal · 2023
    Review
  12. Article
  13. Article
  14. Review
  15. Article
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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

8 authors.

Kevin CarvalhoCentre de Recherche, Institut Curie, , Paris 75248, France.
Joël Lemière
Fahima Faqir
John Manzi
Laurent Blanchoin
Julie Plastino
Timo Betz
Cécile Sykes

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Cells use complex biochemical pathways to drive shape changes for polarization and movement. One of these pathways is the self-assembly of actin filaments and myosin motors that together produce the forces and tensions that drive cell shape changes. Whereas the role of actin and myosin motors in cell polarization is clear, the exact mechanism of how the cortex, a thin shell of actin that is underneath the plasma membrane, can drive cell shape changes is still an open question. Here, we address this issue using biomimetic systems: the actin cortex is reconstituted on liposome membranes, in an 'outside geometry'. The actin shell is either grown from an activator of actin polymerization immobilized at the membrane by a biotin-streptavidin link, or built by simple adsorption of biotinylated actin filaments to the membrane, in the presence or absence of myosin motors. We show that tension in the actin network can be induced either by active actin polymerization on the membrane via the Arp2/3 complex or by myosin II filament pulling activity. Symmetry breaking and spontaneous polarization occur above a critical tension that opens up a crack in the actin shell. We show that this critical tension is reached by growing branched networks, nucleated by the Arp2/3 complex, in a concentration window of capping protein that limits actin filament growth and by a sufficient number of motors that pull on actin filaments. Our study provides the groundwork to understanding the physical mechanisms at work during polarization prior to cell shape modifications.

Indexed as

Models, BiologicalPolymerizationActin-Related Protein 2-3 ComplexActinsBiomechanical PhenomenaBiomimeticsBiotinCell MovementCell PolarityCell ShapeHumansLiposomesMyosin Type IIProfilinsStreptavidinActin-Related Protein 2-3 ComplexActinsBiotinLiposomesMyosin Type IIProfilinsStreptavidinacto-myosinbiomimetic liposomecortical tensionsymmetry breaking

Identifiers

PMID24062578
PMCPMC3785958

What OpenQuestion holds

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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.