Evidence map›Paper›PMID 28008977›Full record

ArticleScientific reports2016

Differential identity of Filopodia and Tunneling Nanotubes revealed by the opposite functions of actin regulatory complexes.

Elise Delage, Diégo Cordero Cervantes, Esthel Pénard, Christine Schmitt, Sylvie Syan, Andrea Disanza, Giorgio Scita, Chiara Zurzolo

Open access · goldAbstract read
In one paragraph

Article in Scientific reports, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 87 papers.

0numbers the graph read from it
0cells of the map it votes in
87citing papers in PubMed
6.6field-weighted citation impact, top 3% 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

87 citing papers in PubMed, 130 citations in OpenAlex.

  1. Review
  2. Review
  3. The molecular architecture of tunneling nanotubes.bioRxiv : the preprint server for biology · 2026
    Article
  4. Building the bridges: molecular mechanisms of tunneling nanotube formation.Cellular and molecular life sciences : CMLS · 2026
    Review
  5. Review
  6. ImpairedNature communications · 2026
    Article
  7. Article
  8. Article
  9. Review
  10. Review
  11. Review
  12. Beyond synapses: cytoplasmic connections in brain function and evolution.Biological reviews of the Cambridge Philosophical Society · 2025
    Review
  13. Article
  14. Review
  15. Article
  16. Review
  17. Article
  18. Review
  19. Review
  20. Review

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

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

8 authors at 2 institutions in 2 countries.

Elise DelageUnité Trafic Membranaire et Pathogenèse, Institut Pasteur, 25-28 Rue du Docteur Roux, 75724 Paris CEDEX 15, France.
Diégo Cordero CervantesUnité Trafic Membranaire et Pathogenèse, Institut Pasteur, 25-28 Rue du Docteur Roux, 75724 Paris CEDEX 15, France.
Esthel PénardUnité Trafic Membranaire et Pathogenèse, Institut Pasteur, 25-28 Rue du Docteur Roux, 75724 Paris CEDEX 15, France.
Christine SchmittUltrapole, Institut Pasteur, 25-28 Rue du Docteur Roux, 75724 Paris CEDEX 15, France.
Sylvie SyanUnité Trafic Membranaire et Pathogenèse, Institut Pasteur, 25-28 Rue du Docteur Roux, 75724 Paris CEDEX 15, France.
Andrea DisanzaFIRC Institute of Molecular Oncology, 20139 Milan, Italy.
Giorgio ScitaFIRC Institute of Molecular Oncology, 20139 Milan, Italy.
Chiara ZurzoloUnité Trafic Membranaire et Pathogenèse, Institut Pasteur, 25-28 Rue du Docteur Roux, 75724 Paris CEDEX 15, France.
Institut Pasteur · FRFIRC Institute of Molecular Oncology · IT

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Tunneling Nanotubes (TNTs) are actin enriched filopodia-like protrusions that play a pivotal role in long-range intercellular communication. Different pathogens use TNT-like structures as "freeways" to propagate across cells. TNTs are also implicated in cancer and neurodegenerative diseases, making them promising therapeutic targets. Understanding the mechanism of their formation, and their relation with filopodia is of fundamental importance to uncover their physiological function, particularly since filopodia, differently from TNTs, are not able to mediate transfer of cargo between distant cells. Here we studied different regulatory complexes of actin, which play a role in the formation of both these structures. We demonstrate that the filopodia-promoting CDC42/IRSp53/VASP network negatively regulates TNT formation and impairs TNT-mediated intercellular vesicle transfer. Conversely, elevation of Eps8, an actin regulatory protein that inhibits the extension of filopodia in neurons, increases TNT formation. Notably, Eps8-mediated TNT induction requires Eps8 bundling but not its capping activity. Thus, despite their structural similarities, filopodia and TNTs form through distinct molecular mechanisms. Our results further suggest that a switch in the molecular composition in common actin regulatory complexes is critical in driving the formation of either type of membrane protrusion.

Indexed as

Actin CytoskeletonActinsAdaptor Proteins, Signal TransducingAnimalsBraincdc42 GTP-Binding ProteinCell Adhesion MoleculesCell CommunicationCell MembraneEndocytosisGreen Fluorescent ProteinsMiceMicrofilament ProteinsMicroscopy, Electron, ScanningNanotubesNerve Tissue ProteinsActinsAdaptor Proteins, Signal TransducingBaiap2 protein, mousecdc42 GTP-Binding ProteinCdc42 protein, mouseCell Adhesion MoleculesEps8 protein, mouseGreen Fluorescent ProteinsMicrofilament ProteinsNerve Tissue ProteinsPhosphoproteinsVasodilator-Stimulated Phosphoprotein

Identifiers

PMID28008977
PMCPMC5180355
OpenAlexW2616668499

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.