Evidence map›Paper›PMID 26655834›Full record

ArticleNature cell biology2016

Isoform diversity in the Arp2/3 complex determines actin filament dynamics.

Jasmine V G Abella, Chiara Galloni, Julien Pernier, David J Barry, Svend Kjær, Marie-France Carlier, Michael Way

Abstract read
PubMed Publisher
In one paragraph

Article in Nature cell biology, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 125 papers.

0numbers the graph read from it
0cells of the map it votes in
125citing papers in PubMed
7.2field-weighted citation impact, top 2% 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

125 citing papers in PubMed, 216 citations in OpenAlex.

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65 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

7 authors at 2 institutions in 2 countries.

Jasmine V G AbellaCellular Signalling and Cytoskeletal Function, The Francis Crick Institute, Lincoln's Inn Fields Laboratory, 44 Lincoln's Inn Fields, London, WC2A 3LY, UK.
Chiara GalloniCellular Signalling and Cytoskeletal Function, The Francis Crick Institute, Lincoln's Inn Fields Laboratory, 44 Lincoln's Inn Fields, London, WC2A 3LY, UK.
Julien PernierLaboratoire d'Enzymologie et Biochimie Structurale, I2BC, CNRS, 91198 Gif-sur-Yvette, France.
David J BarryCellular Signalling and Cytoskeletal Function, The Francis Crick Institute, Lincoln's Inn Fields Laboratory, 44 Lincoln's Inn Fields, London, WC2A 3LY, UK.
Svend KjærThe Structural Biology Science Technology Platform, The Francis Crick Institute, Lincoln's Inn Fields Laboratory, 44 Lincoln's Inn Fields, London, WC2A 3LY, UK.
Marie-France CarlierLaboratoire d'Enzymologie et Biochimie Structurale, I2BC, CNRS, 91198 Gif-sur-Yvette, France.
Michael WayCellular Signalling and Cytoskeletal Function, The Francis Crick Institute, Lincoln's Inn Fields Laboratory, 44 Lincoln's Inn Fields, London, WC2A 3LY, UK.
Cytoskeleton (United States) · USInstitut de Biologie Intégrative de la Cellule · FR

Funding

Canadian Institutes of Health ResearchCancer Research UK
6 · The paper itself

Abstract

The Arp2/3 complex consists of seven evolutionarily conserved subunits (Arp2, Arp3 and ARPC1-5) and plays an essential role in generating branched actin filament networks during many different cellular processes. In mammals, however, the ARPC1 and ARPC5 subunits are each encoded by two isoforms that are 67% identical. This raises the possibility that Arp2/3 complexes with different properties may exist.  We found that Arp2/3 complexes containing ARPC1B and ARPC5L are significantly better at promoting actin assembly than those with ARPC1A and ARPC5, both in cells and in vitro. Branched actin networks induced by complexes containing ARPC1B or ARPC5L are also disassembled ∼2-fold slower than those formed by their counterparts. This difference reflects the ability of cortactin to stabilize ARPC1B- and ARPC5L- but not ARPC1A- and ARPC5-containing complexes against coronin-mediated disassembly. Our observations demonstrate that the Arp2/3 complex in higher eukaryotes is actually a family of complexes with different properties.

Indexed as

Actin CytoskeletonActin-Related Protein 2Actin-Related Protein 3Angiopoietin-Like Protein 2Angiopoietin-like ProteinsAngiopoietinsAnimalsCell LineCortactinHumansMiceMicrofilament ProteinsProtein IsoformsActin-Related Protein 2Actin-Related Protein 3ACTR2 protein, humanACTR3 protein, humanActr3 protein, mouseAngiopoietin-Like Protein 2Angiopoietin-like ProteinsAngiopoietinsAngptl2 protein, mousecoronin proteinsCortactinCTTN protein, humanCttn protein, mouseMicrofilament ProteinsProtein Isoforms

Identifiers

PMID26655834
OpenAlexW2212184159

What OpenQuestion holds

Textmetadata
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.