Evidence map›Paper›PMID 25598228›Full record

ArticleScientific reports2015

The role of myosin-II in force generation of DRG filopodia and lamellipodia.

Wasim A Sayyad, Ladan Amin, Paolo Fabris, Erika Ercolini, Vincent Torre

Open access · goldAbstract read
In one paragraph

Article in Scientific reports, 2015. 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
2.7field-weighted citation impact, top 11% 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, 37 citations in OpenAlex.

  1. Myosin II-independent contraction of actin filaments in membrane nanotubes.Proceedings of the National Academy of Sciences of the United States of America · 2026
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  11. Mechanics of Pollen Tube Elongation: A Perspective.Frontiers in plant science · 2020
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  14. Axon growth regulation by a bistable molecular switch.Proceedings. Biological sciences · 2018
    Article
  15. Article
  16. Review
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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 1 institution in 1 country.

Wasim A SayyadNeuroscience Area, International School for Advanced Studies (SISSA), IT-34136 Trieste, Italy.
Ladan AminNeuroscience Area, International School for Advanced Studies (SISSA), IT-34136 Trieste, Italy.
Paolo FabrisNeuroscience Area, International School for Advanced Studies (SISSA), IT-34136 Trieste, Italy.
Erika ErcoliniNeuroscience Area, International School for Advanced Studies (SISSA), IT-34136 Trieste, Italy.
Vincent TorreNeuroscience Area, International School for Advanced Studies (SISSA), IT-34136 Trieste, Italy.
Scuola Internazionale Superiore di Studi Avanzati · IT

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Differentiating neurons process the mechanical stimulus by exerting the protrusive forces through lamellipodia and filopodia. We used optical tweezers, video imaging and immunocytochemistry to analyze the role of non-muscle myosin-II on the protrusive force exerted by lamellipodia and filopodia from developing growth cones (GCs) of isolated Dorsal Root Ganglia (DRG) neurons. When the activity of myosin-II was inhibited by 30 μM Blebbistatin protrusion/retraction cycles of lamellipodia slowed down and during retraction lamellipodia could not lift up axially as in control condition. Inhibition of actin polymerization with 25 nM Cytochalasin-D and of microtubule polymerization with 500 nM Nocodazole slowed down the protrusion/retraction cycles, but only Cytochalasin-D decreased lamellipodia axial motion. The force exerted by lamellipodia treated with Blebbistatin decreased by 50%, but, surprisingly, the force exerted by filopodia increased by 20-50%. The concomitant disruption of microtubules caused by Nocodazole abolished the increase of the force exerted by filopodia treated with Blebbistatin. These results suggest that; i- Myosin-II controls the force exerted by lamellipodia and filopodia; ii- contractions of the actomyosin complex formed by filaments of actin and myosin have an active role in ruffle formation; iii- myosin-II is an essential component of the structural stability of GCs architecture.

Indexed as

AnimalsCytochalasin DGanglia, SpinalHeterocyclic Compounds, 4 or More RingsMicroscopy, FluorescenceMyosin Heavy ChainsMyosin Type IINeuronsNocodazoleOptical TweezersPseudopodiaRatsRats, WistarTubulinblebbistatinCytochalasin DHeterocyclic Compounds, 4 or More RingsMyosin Heavy ChainsMyosin Type IINocodazoleTubulin

Identifiers

PMID25598228
PMCPMC4648386
OpenAlexW2054590902

What OpenQuestion holds

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LicenceCC BY-NC-SA
Read underepoch 390

Registered trials

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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.