Evidence map›Paper›PMID 28007915›Full record

ArticleThe Journal of cell biology2017

Podosome assembly is controlled by the GTPase ARF1 and its nucleotide exchange factor ARNO.

Nisha Bte Mohd Rafiq, Zi Zhao Lieu, Tingting Jiang, Cheng-Han Yu, Paul Matsudaira, Gareth E Jones, Alexander D Bershadsky

Open access · bronzeAbstract readVideo-Audio Media
In one paragraph

Article in The Journal of cell biology, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.

0numbers the graph read from it
0cells of the map it votes in
28citing papers in PubMed
4.4field-weighted citation impact, top 6% 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

28 citing papers in PubMed, 48 citations in OpenAlex.

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  12. Asap1 Affects the Susceptibility of Zebrafish toFrontiers in cellular and infection microbiology · 2020
    Article
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  19. Forces and constraints controlling podosome assembly and disassembly.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2019
    Article
  20. Review
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

7 authors at 2 institutions in 3 countries.

Nisha Bte Mohd RafiqMechanobiology Institute, National University of Singapore, Singapore 117411, Singapore.ORCID http://orcid.org/0000-0002-4434-0504
Zi Zhao LieuMechanobiology Institute, National University of Singapore, Singapore 117411, Singapore.
Tingting JiangMechanobiology Institute, National University of Singapore, Singapore 117411, Singapore.
Cheng-Han YuMechanobiology Institute, National University of Singapore, Singapore 117411, Singapore.ORCID http://orcid.org/0000-0002-8821-8877
Paul MatsudairaMechanobiology Institute, National University of Singapore, Singapore 117411, Singapore.ORCID http://orcid.org/0000-0002-8399-3276
Gareth E JonesRandall Division of Cell and Molecular Biophysics, King's College London, London SE1 1UL, England, UK alexander.bershadsky@weizmann.ac.il gareth.jones@kcl.ac.uk.ORCID http://orcid.org/0000-0001-5879-3048
Alexander D BershadskyMechanobiology Institute, National University of Singapore, Singapore 117411, Singapore alexander.bershadsky@weizmann.ac.il gareth.jones@kcl.ac.uk.ORCID http://orcid.org/0000-0002-9571-7375
National University of Singapore · SGKing's College London · GB

Funding

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

Abstract

Podosomes represent a class of integrin-mediated cell-matrix adhesions formed by migrating and matrix-degrading cells. We demonstrate that in macrophage-like THP1 cells and fibroblasts stimulated to produce podosomes, down-regulation of the G-protein ARF1 or the ARF1 guanine nucleotide exchange factor, ARNO, by small, interfering RNA or pharmacological inhibitors led to striking podosome elimination. Concomitantly, treatments inducing podosome formation increased the level of guanosine triphosphate (GTP)-bound ARF1. ARNO was found to colocalize with the adhesive rings of podosomes, whereas ARF1 was localized to vesicular structures transiently contacting podosome rings. Inhibition of ARF1 led to an increase in RhoA-GTP levels and triggered assembly of myosin-IIA filaments in THP1 cells, whereas the suppression of myosin-IIA rescued podosome formation regardless of ARF1 inhibition. Finally, expression of constitutively active ARF1 in fibroblasts induced formation of putative podosome precursors: actin-rich puncta coinciding with matrix degradation sites and containing proteins of the podosome core but not of the adhesive ring. Thus, ARNO-ARF1 regulates formation of podosomes by inhibition of RhoA/myosin-II and promotion of actin core assembly.

Indexed as

Actin CytoskeletonActinsADP-Ribosylation Factor 1AnimalsCell Line, TumorEnzyme InhibitorsGTPase-Activating ProteinsGuanosine TriphosphateHumansMiceMicroscopy, FluorescenceNonmuscle Myosin Type IIAPodosomesRecombinant Fusion ProteinsrhoA GTP-Binding Proteinrho-Associated KinasesActinsADP-Ribosylation Factor 1cytohesin-2Enzyme InhibitorsGTPase-Activating ProteinsGuanosine TriphosphateNonmuscle Myosin Type IIARecombinant Fusion ProteinsrhoA GTP-Binding ProteinRHOA protein, humanrho-Associated Kinases

Identifiers

PMID28007915
PMCPMC5223603
OpenAlexW2573495436

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.