Evidence map›Paper›PMID 23555988›Full record

ArticlePloS one2013

IRSp53 mediates podosome formation via VASP in NIH-Src cells.

Tsukasa Oikawa, Hitomi Okamura, Franziska Dietrich, Yosuke Senju, Tadaomi Takenawa, Shiro Suetsugu

Open access · goldAbstract read
In one paragraph

Article in PloS one, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.

0numbers the graph read from it
0cells of the map it votes in
11citing papers in PubMed
0.7field-weighted citation impact, top 33% 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

11 citing papers in PubMed, 19 citations in OpenAlex.

  1. Immune cells fold and damage fungal hyphae.Proceedings of the National Academy of Sciences of the United States of America · 2021
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  7. Mechanism of IRSp53 inhibition by 14-3-3.Nature communications · 2019
    Article
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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

6 authors at 4 institutions in 2 countries.

Tsukasa OikawaLaboratory of Cell and Tissue Biology, Keio University School of Medicine, Sinjuku, Tokyo, Japan.
Hitomi Okamura
Franziska Dietrich
Yosuke Senju
Tadaomi Takenawa
Shiro Suetsugu
The University of Tokyo · JPKeio University · JPKobe University · JPUniversity of Duisburg-Essen · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Podosomes are cellular "feet," characterized by F-actin-rich membrane protrusions, which drive cell migration and invasion into the extracellular matrix. Small GTPases that regulate the actin cytoskeleton, such as Cdc42 and Rac are central regulators of podosome formation. The adaptor protein IRSp53 contains an I-BAR domain that deforms membranes into protrusions and binds to Rac, a CRIB motif that interacts with Cdc42, an SH3 domain that binds to many actin cytoskeletal regulators with proline-rich peptides including VASP, and the C-terminal variable region by splicing. However, the role of IRSp53 and VASP in podosome formation had been unclear. Here we found that the knockdown of IRSp53 by RNAi attenuates podosome formation and migration in Src-transformed NIH3T3 (NIH-Src) cells. Importantly, the differences in the IRSp53 C-terminal splicing isoforms did not affect podosome formation. Overexpression of IRSp53 deletion mutants suggested the importance of linking small GTPases to SH3 binding partners. Interestingly, VASP physically interacted with IRSp53 in NIH-Src cells and was essential for podosome formation. These data highlight the role of IRSp53 as a linker of small GTPases to VASP for podosome formation.

Indexed as

Cell MovementActinsAnimalsCell Adhesion MoleculesMiceMicrofilament ProteinsMonomeric GTP-Binding ProteinsNerve Tissue ProteinsNIH 3T3 CellsPhosphoproteinsProtein IsoformsPseudopodiaRNA InterferenceRNA, Small Interferingsrc-Family Kinasessrc Homology DomainsActinsBaiap2 protein, mouseCell Adhesion MoleculesMicrofilament ProteinsMonomeric GTP-Binding ProteinsNerve Tissue ProteinsPhosphoproteinsProtein IsoformsRNA, Small Interferingsrc-Family KinasesVasodilator-Stimulated Phosphoprotein

Identifiers

PMID23555988
PMCPMC3608619
OpenAlexW1963942263

What OpenQuestion holds

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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.