Evidence map›Paper›PMID 32294157›Full record

ArticleThe Journal of cell biology2020

FMNL2 regulates dynamics of fascin in filopodia.

Karin Pfisterer, James Levitt, Campbell D Lawson, Richard J Marsh, John M Heddleston, Eric Wait, Simon Morris Ameer-Beg, Susan Cox, Maddy Parsons

Open access · hybridAbstract read
In one paragraph

Article in The Journal of cell biology, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.

0numbers the graph read from it
0cells of the map it votes in
22citing papers in PubMed
3.1field-weighted citation impact, top 8% 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

22 citing papers in PubMed, 38 citations in OpenAlex.

  1. Article
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  4. Identification of an FMNL2 Interactome by Quantitative Mass Spectrometry.International journal of molecular sciences · 2024
    Article
  5. Article
  6. Imaging actin organisation and dynamics in 3D.Journal of cell science · 2024
    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

9 authors at 2 institutions in 2 countries.

Karin PfistererRandall Centre for Cell and Molecular Biophysics, King's College London, Guy's Campus, London, UK.
James LevittRandall Centre for Cell and Molecular Biophysics, King's College London, Guy's Campus, London, UK.
Campbell D LawsonRandall Centre for Cell and Molecular Biophysics, King's College London, Guy's Campus, London, UK.
Richard J MarshRandall Centre for Cell and Molecular Biophysics, King's College London, Guy's Campus, London, UK.
John M HeddlestonAdvanced Imaging Centre, Howard Hughes Medical Institute, Janelia Research Campus, Ashburn, VA.
Eric WaitAdvanced Imaging Centre, Howard Hughes Medical Institute, Janelia Research Campus, Ashburn, VA.
Simon Morris Ameer-BegRandall Centre for Cell and Molecular Biophysics, King's College London, Guy's Campus, London, UK.
Susan CoxRandall Centre for Cell and Molecular Biophysics, King's College London, Guy's Campus, London, UK.
Maddy ParsonsRandall Centre for Cell and Molecular Biophysics, King's College London, Guy's Campus, London, UK.
King's College London · GBHoward Hughes Medical Institute · US

Funding

Cancer Research UK 21840Howard Hughes Medical InstituteMedical Research Council MR/K015664/1
6 · The paper itself

Abstract

Filopodia are peripheral F-actin-rich structures that enable cell sensing of the microenvironment. Fascin is an F-actin-bundling protein that plays a key role in stabilizing filopodia to support efficient adhesion and migration. Fascin is also highly up-regulated in human cancers, where it increases invasive cell behavior and correlates with poor patient prognosis. Previous studies have shown that fascin phosphorylation can regulate F-actin bundling, and that this modification can contribute to subcellular fascin localization and function. However, the factors that regulate fascin dynamics within filopodia remain poorly understood. In the current study, we used advanced live-cell imaging techniques and a fascin biosensor to demonstrate that fascin phosphorylation, localization, and binding to F-actin are highly dynamic and dependent on local cytoskeletal architecture in cells in both 2D and 3D environments. Fascin dynamics within filopodia are under the control of formins, and in particular FMNL2, that binds directly to dephosphorylated fascin. Our data provide new insight into control of fascin dynamics at the nanoscale and into the mechanisms governing rapid cytoskeletal adaptation to environmental changes. This filopodia-driven exploration stage may represent an essential regulatory step in the transition from static to migrating cancer cells.

Indexed as

ActinsBiosensing TechniquesCarrier ProteinsCell AdhesionCell MovementCellular MicroenvironmentForminsHeLa CellsHumansMicrofilament ProteinsMolecular ImagingNeoplasmsPhosphorylationProtein BindingPseudopodiaActinsCarrier ProteinsfascinFMNL2 protein, humanForminsMicrofilament Proteins

Identifiers

PMID32294157
PMCPMC7199847
OpenAlexW3015773696

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.