Evidence map›Paper›PMID 26446836›Full record

ArticleMolecular biology of the cell2015

Cell type-dependent mechanisms for formin-mediated assembly of filopodia.

Lorna E Young, Ernest G Heimsath, Henry N Higgs

Open access · greenAbstract read
In one paragraph

Article in Molecular biology of the cell, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 35 papers.

0numbers the graph read from it
0cells of the map it votes in
35citing papers in PubMed
3.0field-weighted citation impact, top 9% 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

35 citing papers in PubMed, 56 citations in OpenAlex.

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  9. Building the phagocytic cup on an actin scaffold.Current opinion in cell biology · 2022
    Review
  10. Article
  11. Embedding of HIV Egress within Cortical F-Actin.Pathogens (Basel, Switzerland) · 2022
    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

3 authors at 1 institution in 1 country.

Lorna E YoungDepartment of Biochemistry, Geisel School of Medicine at Dartmouth, Hanover, NH 03755.
Ernest G HeimsathDepartment of Biochemistry, Geisel School of Medicine at Dartmouth, Hanover, NH 03755.
Henry N HiggsDepartment of Biochemistry, Geisel School of Medicine at Dartmouth, Hanover, NH 03755 henry.higgs@dartmouth.edu.
Dartmouth College · US

Funding

Translational Engineering in Cancer (TEC)P30CA023108 · NCI · DARTMOUTH COLLEGE · PI Steven D Leach · 1985 to 2026
$91.3M
Comparative molecular physiology of mammalian forminsR01GM069818 · NIGMS · DARTMOUTH COLLEGE · PI HIGGS, HENRY N · 2004 to 2017
$4.3M
Filopodia assembly by FMNL3: biochemical mechanism and cellular functionR01GM109965 · NIGMS · DARTMOUTH COLLEGE · PI HIGGS, HENRY N · 2015 to 2017
$1.1M
NCI NIH HHS P30 CA023108NIGMS NIH HHS GM069818NIGMS NIH HHS GM109965NIGMS NIH HHS R01 GM069818NIGMS NIH HHS R01 GM109965
6 · The paper itself

Abstract

Filopodia are finger-like protrusions from the plasma membrane and are of fundamental importance to cellular physiology, but the mechanisms governing their assembly are still in question. One model, called convergent elongation, proposes that filopodia arise from Arp2/3 complex-nucleated dendritic actin networks, with factors such as formins elongating these filaments into filopodia. We test this model using constitutively active constructs of two formins, FMNL3 and mDia2. Surprisingly, filopodial assembly requirements differ between suspension and adherent cells. In suspension cells, Arp2/3 complex is required for filopodial assembly through either formin. In contrast, a subset of filopodia remains after Arp2/3 complex inhibition in adherent cells. In adherent cells only, mDia1 and VASP also contribute to filopodial assembly, and filopodia are disproportionately associated with focal adhesions. We propose an extension of the existing models for filopodial assembly in which any cluster of actin filament barbed ends in proximity to the plasma membrane, either Arp2/3 complex dependent or independent, can initiate filopodial assembly by specific formins.

Indexed as

Actin CytoskeletonActin-Related Protein 2-3 ComplexCarrier ProteinsCell Adhesion MoleculesCell MembraneDendritesForminsHumansJurkat CellsMicrofilament ProteinsPhosphoproteinsProteinsPseudopodiaVasodilator-Stimulated PhosphoproteinActin-Related Protein 2-3 ComplexCarrier ProteinsCell Adhesion MoleculesDIAPH2 protein, humanFMNL3 protein, humanForminsMicrofilament ProteinsPhosphoproteinsProteinsVasodilator-Stimulated Phosphoprotein

Identifiers

PMID26446836
PMCPMC4678021
OpenAlexW2220985966

What OpenQuestion holds

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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.