Evidence map›Paper›PMID 23885122›Full record

ArticleMolecular biology of the cell2013

Arp2/3 complex is essential for actin network treadmilling as well as for targeting of capping protein and cofilin.

Stefan A Koestler, Anika Steffen, Maria Nemethova, Moritz Winterhoff, Ningning Luo, J Margit Holleboom, Jessica Krupp, Sonja Jacob, Marlene Vinzenz, Florian Schur and 8 more

Abstract read
In one paragraph

Article in Molecular biology of the cell, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 46 papers.

0numbers the graph read from it
0cells of the map it votes in
46citing papers in PubMed
4.4field-weighted citation impact, top 5% 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

46 citing papers in PubMed, 78 citations in OpenAlex.

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  20. Actin cytoskeleton in mesenchymal-to-amoeboid transition of cancer cells.International review of cell and molecular biology · 2020
    Review
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

18 authors at 8 institutions in 3 countries.

Stefan A KoestlerInstitute of Genetics, University of Bonn, D-53115 Bonn, Germany Institute of Molecular Biotechnology, Austrian Academy of Sciences, A-1030 Vienna, Austria Johann Radon Institute for Computational and Applied Mathematics, Austrian Academy of Sciences, A-1030 Vienna, Austria Institute for Biophysical Chemistry, Hannover Medical School, D-30625 Hannover, Germany Helmholtz Centre for Infection Research, D-38124 Braunschweig, Germany Institute for Molecular Cell Biology, University of Münster, D-48149 Münster, Germany Oncology Research Unit, School of Medical Sciences, University of New South Wales, Sydney 2052, Australia Faculty of Mathematics, University of Vienna, A-1090 Vienna, Austria.
Anika Steffen
Maria Nemethova
Moritz Winterhoff
Ningning Luo
J Margit Holleboom
Jessica Krupp
Sonja Jacob
Marlene Vinzenz
Florian Schur
Kai Schlüter
Peter W Gunning
Christoph Winkler
Christian Schmeiser
Jan Faix
Theresia E B Stradal
J Victor Small
Klemens Rottner
Institute of Molecular Biotechnology · ATUniversity of Bonn · DEMedizinische Hochschule Hannover · DEUniversity of Münster · DEAustrian Academy of Sciences · ATHelmholtz Centre for Infection Research · DEUniversity of Vienna · ATUNSW Sydney · AU

Funding

Austrian Science Fund FWF I 516
6 · The paper itself

Abstract

Lamellipodia are sheet-like protrusions formed during migration or phagocytosis and comprise a network of actin filaments. Filament formation in this network is initiated by nucleation/branching through the actin-related protein 2/3 (Arp2/3) complex downstream of its activator, suppressor of cAMP receptor/WASP-family verprolin homologous (Scar/WAVE), but the relative relevance of Arp2/3-mediated branching versus actin filament elongation is unknown. Here we use instantaneous interference with Arp2/3 complex function in live fibroblasts with established lamellipodia. This allows direct examination of both the fate of elongating filaments upon instantaneous suppression of Arp2/3 complex activity and the consequences of this treatment on the dynamics of other lamellipodial regulators. We show that Arp2/3 complex is an essential organizer of treadmilling actin filament arrays but has little effect on the net rate of actin filament turnover at the cell periphery. In addition, Arp2/3 complex serves as key upstream factor for the recruitment of modulators of lamellipodia formation such as capping protein or cofilin. Arp2/3 complex is thus decisive for filament organization and geometry within the network not only by generating branches and novel filament ends, but also by directing capping or severing activities to the lamellipodium. Arp2/3 complex is also crucial to lamellipodia-based migration of keratocytes.

Indexed as

Actin Capping ProteinsActin CytoskeletonActin Depolymerizing FactorsActin-Related Protein 2-3 ComplexActinsAnimalsCell MembraneEpidermal CellsFibroblastsFishesMiceMicroinjectionsMyosin Type IINIH 3T3 CellsProtein Structure, TertiaryPseudopodiaActin Capping ProteinsActin Depolymerizing FactorsActin-Related Protein 2-3 ComplexActinsMyosin Type IIWiskott-Aldrich Syndrome Protein Family

Identifiers

PMID23885122
PMCPMC3771948
OpenAlexW2103501363

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-SA
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.