Evidence map›Paper›PMID 28194011›Full record

ArticleNature communications2017

Self-organizing actin patterns shape membrane architecture but not cell mechanics.

M Fritzsche, D Li, H Colin-York, V T Chang, E Moeendarbary, J H Felce, E Sezgin, G Charras, E Betzig, C Eggeling

Abstract read
In one paragraph

Article in Nature communications, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 61 papers.

0numbers the graph read from it
0cells of the map it votes in
61citing 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

61 citing papers in PubMed.

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  14. A census of actin-associated proteins in humans.Frontiers in cell and developmental biology · 2023
    Article
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1 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

10 authors.

M FritzscheMRC Human Immunology Unit, Weatherall Institute of Molecular Medicine, University of Oxford, Headley Way, Oxford OX3 9DS, UK.
D LiNational Laboratory of Biomacromolecules, Institute of Biophysics, Chinese Academy of Sciences, Beijing 100101, China.
H Colin-YorkMRC Human Immunology Unit, Weatherall Institute of Molecular Medicine, University of Oxford, Headley Way, Oxford OX3 9DS, UK.
V T ChangMRC Human Immunology Unit, Weatherall Institute of Molecular Medicine, University of Oxford, Headley Way, Oxford OX3 9DS, UK.
E MoeendarbaryDepartment of Biological Engineering, Massachusetts Institute of Technology, Cambridge, Massachusetts 02142, USA.
J H FelceMRC Human Immunology Unit, Weatherall Institute of Molecular Medicine, University of Oxford, Headley Way, Oxford OX3 9DS, UK.
E SezginMRC Human Immunology Unit, Weatherall Institute of Molecular Medicine, University of Oxford, Headley Way, Oxford OX3 9DS, UK.ORCID 0000-0002-4915-388X
G CharrasLondon Centre for Nanotechnology and Department of Cell &Developmental Biology, University College London, 17-19 Gordon Street, London WC1H 0AH, UK.
E BetzigHoward Hughes Medical Institute, Janelia Research Campus, 19700 Helix Drive, Ashburn, Virginia 20147, USA.
C EggelingMRC Human Immunology Unit, Weatherall Institute of Molecular Medicine, University of Oxford, Headley Way, Oxford OX3 9DS, UK.

Funding

Medical Research Council G0902418Medical Research Council MC_UU_00008/9Medical Research Council MC_UU_12010/9Medical Research Council MR/K01577X/1
6 · The paper itself

Abstract

Cell-free studies have demonstrated how collective action of actin-associated proteins can organize actin filaments into dynamic patterns, such as vortices, asters and stars. Using complementary microscopic techniques, we here show evidence of such self-organization of the actin cortex in living HeLa cells. During cell adhesion, an active multistage process naturally leads to pattern transitions from actin vortices over stars into asters. This process is primarily driven by Arp2/3 complex nucleation, but not by myosin motors, which is in contrast to what has been theoretically predicted and observed in vitro. Concomitant measurements of mechanics and plasma membrane fluidity demonstrate that changes in actin patterning alter membrane architecture but occur functionally independent of macroscopic cortex elasticity. Consequently, tuning the activity of the Arp2/3 complex to alter filament assembly may thus be a mechanism allowing cells to adjust their membrane architecture without affecting their macroscopic mechanical properties.

Indexed as

Membrane FluidityActin CytoskeletonActin-Related Protein 2-3 ComplexActinsCell AdhesionCell MembraneHEK293 CellsHeLa CellsHumansMechanical PhenomenaMicroscopy, Atomic ForceMicroscopy, Electron, ScanningMicroscopy, FluorescenceModels, MolecularProtein ConformationActin-Related Protein 2-3 ComplexActins

Identifiers

PMID28194011
PMCPMC5316839

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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.