Evidence map›Paper›PMID 25086067›Full record

ArticleJournal of cell science2014

A crucial role for β2 integrins in podosome formation, dynamics and Toll-like-receptor-signaled disassembly in dendritic cells.

Christian Gawden-Bone, Michele A West, Vicky L Morrison, Alexander J Edgar, Sarah J McMillan, Brian D Dill, Matthias Trost, Alan Prescott, Susanna C Fagerholm, Colin Watts

Open access · hybridAbstract read
In one paragraph

Article in Journal of cell science, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.

0numbers the graph read from it
0cells of the map it votes in
21citing papers in PubMed
1.6field-weighted citation impact, top 18% 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

21 citing papers in PubMed, 41 citations in OpenAlex.

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  12. The role of βBMC immunology · 2021
    Article
  13. Visualization of integrin molecules by fluorescence imaging and techniques.Biocell : official journal of the Sociedades Latinoamericanas de Microscopia Electronica ... et. al · 2021
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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

10 authors at 2 institutions in 1 country.

Christian Gawden-BoneDivision of Cell Biology and Immunology, College of Life Sciences, University of Dundee, Dundee DD1 5EH, UK.
Michele A WestDivision of Cell Biology and Immunology, College of Life Sciences, University of Dundee, Dundee DD1 5EH, UK.
Vicky L MorrisonUniversity of Dundee, Ninewells Hospital and Medical School, Dundee DD1 9SY, UK.
Alexander J EdgarDivision of Cell Biology and Immunology, College of Life Sciences, University of Dundee, Dundee DD1 5EH, UK.
Sarah J McMillanDivision of Cell Biology and Immunology, College of Life Sciences, University of Dundee, Dundee DD1 5EH, UK.
Brian D DillMRC Protein Phosphorylation and Ubiquitylation Unit, College of Life Sciences, University of Dundee, Dundee DD1 5EH, UK.
Matthias TrostMRC Protein Phosphorylation and Ubiquitylation Unit, College of Life Sciences, University of Dundee, Dundee DD1 5EH, UK.
Alan PrescottDivision of Cell Biology and Immunology, College of Life Sciences, University of Dundee, Dundee DD1 5EH, UK.
Susanna C FagerholmUniversity of Dundee, Ninewells Hospital and Medical School, Dundee DD1 9SY, UK.
Colin WattsDivision of Cell Biology and Immunology, College of Life Sciences, University of Dundee, Dundee DD1 5EH, UK c.watts@dundee.ac.uk.
University of Dundee · GBNinewells Hospital · GB

Funding

Biotechnology and Biological Sciences Research Council BB/G017123/1Medical Research Council G0701272Medical Research Council G1100713Medical Research Council MC_UP_A500_1020Medical Research Council MC_UU_12016/5
6 · The paper itself

Abstract

The dynamic properties of podosomes, their ability to degrade the underlying matrix and their modulation by Toll-like receptor (TLR) signaling in dendritic cells (DCs) suggests they have an important role in migration. Integrins are thought to participate in formation and dynamics of podosomes but the multiplicity of integrins in podosomes has made this difficult to assess. We report that murine DCs that lack β2 integrins fail to form podosomes. Re-expression of β2 integrins restored podosomes but not when the membrane proximal or distal NPxF motifs, or when an intervening triplet of threonine residues were mutated. We show that β2 integrins are remarkably long-lived in podosome clusters and form a persistent framework that hosts multiple actin-core-formation events at the same or adjacent sites. When β2 integrin amino acid residues 745 or 756 were mutated from Ser to Ala, podosomes became resistant to dissolution mediated through TLR signaling. TLR signaling did not detectably modulate phosphorylation at these sites but mutation of either residue to phospho-mimetic Asp increased β2 integrin turnover in podosomes, indicating that phosphorylation at one or both sites establishes permissive conditions for TLR-signaled podosome disassembly.

Indexed as

AnimalsCD18 AntigensCell Membrane StructuresCell MovementDendritic CellsFemaleMiceMice, Inbred C57BLPregnancySignal TransductionToll-Like ReceptorsCD18 AntigensToll-Like ReceptorsDendritic cellsIntegrinsPodosomes

Identifiers

PMID25086067
PMCPMC4179490
OpenAlexW2099060728

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.