Evidence map›Paper›PMID 25413351›Full record

ArticleJournal of cell science2015

Tyrosine phosphorylation of WIP releases bound WASP and impairs podosome assembly in macrophages.

Vineetha Vijayakumar, James Monypenny, Xing Judy Chen, Laura M Machesky, Sergio Lilla, Adrian J Thrasher, Inés M Antón, Yolanda Calle, Gareth E Jones

Open access · hybridAbstract read
In one paragraph

Article in Journal of cell science, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.

0numbers the graph read from it
0cells of the map it votes in
14citing papers in PubMed
0.9field-weighted citation impact, top 27% 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

14 citing papers in PubMed, 21 citations in OpenAlex.

  1. Plasticity in leukocyte migration during haematopoiesis and inflammation.Journal of muscle research and cell motility · 2025
    Review
  2. Cells · 2022
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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

9 authors at 3 institutions in 2 countries.

Vineetha VijayakumarRandall Division of Cell and Molecular Biophysics, King's College London, London SE1 1UL, UK.
James MonypennyRandall Division of Cell and Molecular Biophysics, King's College London, London SE1 1UL, UK.
Xing Judy ChenRandall Division of Cell and Molecular Biophysics, King's College London, London SE1 1UL, UK.
Laura M MacheskyThe Beatson Institute for Cancer Research, Glasgow G61 1BD, UK.
Sergio LillaThe Beatson Institute for Cancer Research, Glasgow G61 1BD, UK.
Adrian J ThrasherSection of Molecular and Cellular Immunology, Institute of Child Health, University College London, London WC1N 1EH, UK.
Inés M AntónCentro Nacional de Biotecnología (CNB-CSIC), 28049 Madrid, Spain.
Yolanda CalleDepartment of Haematological & Molecular Medicine, King's College London, London SE5 9NU, UK.
Gareth E JonesRandall Division of Cell and Molecular Biophysics, King's College London, London SE1 1UL, UK gareth.jones@kcl.ac.uk.
King's College London · GBCancer Research UK Scotland Institute · GBCentro Nacional de Biotecnología · ES

Funding

Cancer Research UK 15673Medical Research Council G1100041Wellcome TrustWellcome Trust 080373
6 · The paper itself

Abstract

Podosomes are integrin-containing adhesion structures commonly found in migrating leukocytes of the monocytic lineage. The actin cytoskeletal organisation of podosomes is based on a WASP- and Arp2/3-mediated mechanism. WASP also associates with a second protein, WIP (also known as WIPF1), and they co-localise in podosome cores. Here, we report for the first time that WIP can be phosphorylated on tyrosine residues and that tyrosine phosphorylation of WIP is a trigger for release of WASP from the WIP-WASP complex. Using a knockdown approach together with expression of WIP phosphomimics, we show that in the absence of WIP-WASP binding, cellular WASP is rapidly degraded, leading to disruption of podosomes and a failure of cells to degrade an underlying matrix. In the absence of tyrosine phosphorylation, the WIP-WASP complex remains intact and podosome lifetimes are extended. A screen of candidate kinases and inhibitor-based assays identified Bruton's tyrosine kinase (Btk) as a regulator of WIP tyrosine phosphorylation. We conclude that tyrosine phosphorylation of WIP is a crucial regulator of WASP stability and function as an actin-nucleation-promoting factor.

Indexed as

Actin CytoskeletonAgammaglobulinaemia Tyrosine KinaseAnimalsCytoskeletal ProteinsExtracellular MatrixHumansIntracellular Signaling Peptides and ProteinsMacrophagesPhosphorylationPodosomesProtein BindingProtein-Tyrosine KinasesTyrosineWiskott-Aldrich Syndrome ProteinAgammaglobulinaemia Tyrosine KinaseBTK protein, humanCytoskeletal ProteinsIntracellular Signaling Peptides and ProteinsProtein-Tyrosine KinasesTyrosineWIPF1 protein, humanWiskott-Aldrich Syndrome ProteinActin cytoskeletonMacrophagesMatrix degradationPodosomeTyrosine phosphorylationWIPWIPF1

Identifiers

PMID25413351
PMCPMC4294773
OpenAlexW2167509975

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.