Evidence map›Paper›PMID 25017211›Full record

ArticleCurrent biology : CB2014

Cellular control of cortical actin nucleation.

Miia Bovellan, Yves Romeo, Maté Biro, Annett Boden, Priyamvada Chugh, Amina Yonis, Malti Vaghela, Marco Fritzsche, Dale Moulding, Richard Thorogate and 6 more

Open access · hybridAbstract read
In one paragraph

Article in Current biology : CB, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 147 papers.

0numbers the graph read from it
0cells of the map it votes in
147citing papers in PubMed
10.5field-weighted citation impact, top 1% 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

147 citing papers in PubMed, 251 citations in OpenAlex.

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  19. Osteoclasts at Bone Remodeling: Order from Order.Results and problems in cell differentiation · 2024
    Review
  20. Article

87 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

16 authors at 6 institutions in 5 countries.

Miia BovellanLondon Centre for Nanotechnology, University College London, London WC1H 0AH, UK; Department of Cell and Developmental Biology, University College London, London WC1E 6BT, UK.
Yves RomeoInstitute for Research in Immunology and Cancer, Université de Montréal, Montréal, QC H3N 3J7, Canada.
Maté BiroMax Planck Institute of Molecular Cell Biology and Genetics, Dresden 01307, Germany; International Institute of Molecular and Cell Biology, Warsaw 02-109, Poland.
Annett BodenMax Planck Institute of Molecular Cell Biology and Genetics, Dresden 01307, Germany; International Institute of Molecular and Cell Biology, Warsaw 02-109, Poland.
Priyamvada ChughMax Planck Institute of Molecular Cell Biology and Genetics, Dresden 01307, Germany; International Institute of Molecular and Cell Biology, Warsaw 02-109, Poland; Medical Research Council Laboratory for Molecular Cell Biology, University College London, London WC1E 6BT, UK.
Amina YonisLondon Centre for Nanotechnology, University College London, London WC1H 0AH, UK; Department of Cell and Developmental Biology, University College London, London WC1E 6BT, UK.
Malti VaghelaLondon Centre for Nanotechnology, University College London, London WC1H 0AH, UK; Department of Physics and Astronomy, University College London, London WC1E 6BT, UK.
Marco FritzscheLondon Centre for Nanotechnology, University College London, London WC1H 0AH, UK; Department of Physics and Astronomy, University College London, London WC1E 6BT, UK.
Dale MouldingInstitute of Child Health, University College London, London WC1N 1EH, UK.
Richard ThorogateLondon Centre for Nanotechnology, University College London, London WC1H 0AH, UK.
Antoine JégouLaboratoire d'Enzymologie et Biochimie Structurales, CNRS, 91198 Gif-sur-Yvette, France.
Adrian J ThrasherInstitute of Child Health, University College London, London WC1N 1EH, UK.
Guillaume Romet-LemonneLaboratoire d'Enzymologie et Biochimie Structurales, CNRS, 91198 Gif-sur-Yvette, France.
Philippe P RouxInstitute for Research in Immunology and Cancer, Université de Montréal, Montréal, QC H3N 3J7, Canada. Electronic address: philippe.roux@umontreal.ca.
Ewa K PaluchMax Planck Institute of Molecular Cell Biology and Genetics, Dresden 01307, Germany; International Institute of Molecular and Cell Biology, Warsaw 02-109, Poland; Medical Research Council Laboratory for Molecular Cell Biology, University College London, London WC1E 6BT, UK. Electronic address: e.paluch@ucl.ac.uk.
Guillaume CharrasLondon Centre for Nanotechnology, University College London, London WC1H 0AH, UK; Department of Cell and Developmental Biology, University College London, London WC1E 6BT, UK. Electronic address: g.charras@ucl.ac.uk.
University College London · GBCentre National de la Recherche Scientifique · FRLondon Centre for Nanotechnology · GBMax Planck Institute of Molecular Cell Biology and Genetics · DEMedical Research Council · GBUniversité de Montréal · CA

Funding

Biotechnology and Biological Sciences Research Council BB/F019769Biotechnology and Biological Sciences Research Council BB/F019769/1Biotechnology and Biological Sciences Research Council BB/F021402Biotechnology and Biological Sciences Research Council BB/F021402/1Medical Research Council MC_UP_1205/1Medical Research Council MC_UU_12018/5Wellcome Trust WT090233
6 · The paper itself

Abstract

The contractile actin cortex is a thin layer of actin, myosin, and actin-binding proteins that subtends the membrane of animal cells. The cortex is the main determinant of cell shape and plays a fundamental role in cell division [1-3], migration [4], and tissue morphogenesis [5]. For example, cortex contractility plays a crucial role in amoeboid migration of metastatic cells [6] and during division, where its misregulation can lead to aneuploidy [7]. Despite its importance, our knowledge of the cortex is poor, and even the proteins nucleating it remain unknown, though a number of candidates have been proposed based on indirect evidence [8-15]. Here, we used two independent approaches to identify cortical actin nucleators: a proteomic analysis using cortex-rich isolated blebs, and a localization/small hairpin RNA (shRNA) screen searching for phenotypes with a weakened cortex or altered contractility. This unbiased study revealed that two proteins generated the majority of cortical actin: the formin mDia1 and the Arp2/3 complex. Each nucleator contributed a similar amount of F-actin to the cortex but had very different accumulation kinetics. Electron microscopy examination revealed that each nucleator affected cortical network architecture differently. mDia1 depletion led to failure in division, but Arp2/3 depletion did not. Interestingly, despite not affecting division on its own, Arp2/3 inhibition potentiated the effect of mDia1 depletion. Our findings indicate that the bulk of the actin cortex is nucleated by mDia1 and Arp2/3 and suggest a mechanism for rapid fine-tuning of cortex structure and mechanics by adjusting the relative contribution of each nucleator.

Indexed as

Actin CytoskeletonActin-Related Protein 2-3 ComplexActinsAdaptor Proteins, Signal TransducingCell DivisionCell Line, TumorCell MembraneCell ShapeCell Surface ExtensionsForminsHeLa CellsHumansMicrofilament ProteinsMicroscopy, Electron, ScanningRNA InterferenceRNA, Small InterferingActin-Related Protein 2-3 ComplexActinsAdaptor Proteins, Signal TransducingDIAPH1 protein, humanForminsMicrofilament ProteinsRNA, Small Interfering

Identifiers

PMID25017211
PMCPMC4110400
OpenAlexW2027681787

What OpenQuestion holds

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LicenceCC BY
Read underepoch 390

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.