Evidence map›Paper›PMID 31431172›Full record

ArticlePhilosophical transactions of the Royal Society of London. Series B, Biological sciences2019

Forces and constraints controlling podosome assembly and disassembly.

Nisha Bte Mohd Rafiq, Gianluca Grenci, Cheng Kai Lim, Michael M Kozlov, Gareth E Jones, Virgile Viasnoff, Alexander D Bershadsky

Open access · bronzeAbstract read
In one paragraph

Article in Philosophical transactions of the Royal Society of London. Series B, Biological sciences, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.

0numbers the graph read from it
0cells of the map it votes in
10citing papers in PubMed
1.9field-weighted citation impact, top 16% 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

10 citing papers in PubMed, 27 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Functional Role of Non-Muscle Myosin II in Microglia: An Updated Review.International journal of molecular sciences · 2021
    Review
  7. Article
  8. Article
  9. Article
  10. The forces of cancer.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2019
    Article
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

7 authors at 3 institutions in 3 countries.

Nisha Bte Mohd RafiqMechanobiology Institute, National University of Singapore, Singapore 117411, Republic of Singapore.
Gianluca GrenciMechanobiology Institute, National University of Singapore, Singapore 117411, Republic of Singapore.
Cheng Kai LimMechanobiology Institute, National University of Singapore, Singapore 117411, Republic of Singapore.
Michael M KozlovDepartment of Physiology and Pharmacology, Sackler Faculty of Medicine, Tel Aviv University, 69978 Tel Aviv, Israel.
Gareth E JonesRandall Centre for Cell and Molecular Biophysics, King's College London, London SE1 1UL, UK.
Virgile ViasnoffMechanobiology Institute, National University of Singapore, Singapore 117411, Republic of Singapore.
Alexander D BershadskyMechanobiology Institute, National University of Singapore, Singapore 117411, Republic of Singapore.
National University of Singapore · SGKing's College London · GBTel Aviv University · IL

Funding

Medical Research Council G1100041Medical Research Council MR/K015664Medical Research Council MR/K015664/1
6 · The paper itself

Abstract

Podosomes are a singular category of integrin-mediated adhesions important in the processes of cell migration, matrix degradation and cancer cell invasion. Despite a wealth of biochemical studies, the effects of mechanical forces on podosome integrity and dynamics are poorly understood. Here, we show that podosomes are highly sensitive to two groups of physical factors. First, we describe the process of podosome disassembly induced by activation of myosin-IIA filament assembly. Next, we find that podosome integrity and dynamics depends upon membrane tension and can be experimentally perturbed by osmotic swelling and deoxycholate treatment. We have also found that podosomes can be disrupted in a reversible manner by single or cyclic radial stretching of the substratum. We show that disruption of podosomes induced by osmotic swelling is independent of myosin-II filaments. The inhibition of the membrane sculpting protein, dynamin-II, but not clathrin, resulted in activation of myosin-IIA filament formation and disruption of podosomes. The effect of dynamin-II inhibition on podosomes was, however, independent of myosin-II filaments. Moreover, formation of organized arrays of podosomes in response to microtopographic cues (the ridges with triangular profile) was not accompanied by reorganization of myosin-II filaments. Thus, mechanical elements such as myosin-II filaments and factors affecting membrane tension/sculpting independently modulate podosome formation and dynamics, underlying a versatile response of these adhesion structures to intracellular and extracellular cues. This article is part of a discussion meeting issue 'Forces in cancer: interdisciplinary approaches in tumour mechanobiology'.

Indexed as

Cell MovementHumansNonmuscle Myosin Type IIAPodosomesTumor Cells, CulturedNonmuscle Myosin Type IIAcell stretchingintegrin-based adhesionsmembrane tensionmyosin-II filamentsstructured-illumination microscopy

Identifiers

PMID31431172
PMCPMC6627021
OpenAlexW2954795572

What OpenQuestion holds

Textmetadata
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.