Evidence map›Paper›PMID 19068115›Full record

ArticleBMC cell biology2008

Arp2/3 complex activity in filopodia of spreading cells.

Simon A Johnston, Jonathan P Bramble, Chun L Yeung, Paula M Mendes, Laura M Machesky

Open access · goldAbstract read
In one paragraph

Article in BMC cell biology, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 37 papers.

0numbers the graph read from it
0cells of the map it votes in
37citing papers in PubMed
2.4field-weighted citation impact, top 12% 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

37 citing papers in PubMed, 70 citations in OpenAlex.

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  13. Cortactin in Epithelial-Mesenchymal Transition.Frontiers in cell and developmental biology · 2020
    Review
  14. Review
  15. Article
  16. Durotaxis by Human Cancer Cells.Biophysical journal · 2019
    Article
  17. Review
  18. Article
  19. 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

5 authors at 3 institutions in 1 country.

Simon A JohnstonUniversity of Birmingham School of Biosciences, Edgbaston, Birmingham, UK. s.a.johnston@bham.ac.uk
Jonathan P Bramble
Chun L Yeung
Paula M Mendes
Laura M Machesky
The Edgbaston Hospital · GBUniversity of Birmingham · GBUniversity of Leeds · GB

Funding

Biotechnology and Biological Sciences Research CouncilCancer Research UKMedical Research Council G117/569
6 · The paper itself

Abstract

backgroundCells use filopodia to explore their environment and to form new adhesion contacts for motility and spreading. The Arp2/3 complex has been implicated in lamellipodial actin assembly as a major nucleator of new actin filaments in branched networks. The interplay between filopodial and lamellipodial protrusions is an area of much interest as it is thought to be a key determinant of how cells make motility choices.

resultsWe find that Arp2/3 complex localises to dynamic puncta in filopodia as well as lamellipodia of spreading cells. Arp2/3 complex spots do not appear to depend on local adhesion or on microtubules for their localisation but their inclusion in filopodia or lamellipodia depends on the activity of the small GTPase Rac1. Arp2/3 complex spots in filopodia are capable of incorporating monomeric actin, suggesting the presence of available filament barbed ends for polymerisation. Arp2/3 complex in filopodia co-localises with lamellipodial proteins such as capping protein and cortactin. The dynamics of Arp2/3 complex puncta suggests that they are moving bi-directionally along the length of filopodia and that they may be regions of lamellipodial activity within the filopodia.

conclusionWe suggest that filopodia of spreading cells have regions of lamellipodial activity and that this activity affects the morphology and movement of filopodia. Our work has implications for how we understand the interplay between lamellipodia and filopodia and for how actin networks are generated spatially in cells.

Indexed as

Actin CytoskeletonActin-Related Protein 3Angiopoietin-Like Protein 2Angiopoietin-like ProteinsAngiopoietinsAnimalsCell AdhesionCell LineCell MovementCytoplasmFibroblastsFibronectinsMiceNeuropeptidesProtein BindingProtein TransportActin-Related Protein 3Angiopoietin-Like Protein 2Angiopoietin-like ProteinsAngiopoietinsAngptl2 protein, mouseFibronectinsNeuropeptidesrac1 GTP-Binding ProteinRac1 protein, mouserac GTP-Binding Proteins

Identifiers

PMID19068115
PMCPMC2639383
OpenAlexW2074328351

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.