Evidence map›Paper›PMID 31671862›Full record

ArticleCells2019

Absence of the Tks4 Scaffold Protein Induces Epithelial-Mesenchymal Transition-Like Changes in Human Colon Cancer Cells.

Bálint Szeder, Júlia Tárnoki-Zách, Dóra Lakatos, Virág Vas, Gyöngyi Kudlik, Balázs Merő, Kitti Koprivanacz, László Bányai, Lilla Hámori, Gergely Róna and 3 more

Open access · goldAbstract read
In one paragraph

Article in Cells, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.

0numbers the graph read from it
0cells of the map it votes in
15citing papers in PubMed
0.6field-weighted citation impact, top 28% 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

15 citing papers in PubMed, 19 citations in OpenAlex.

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  10. Review
  11. The Role of TKS5 in Chromosome Stability and Bladder Cancer Progression.International journal of molecular sciences · 2022
    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

13 authors at 4 institutions in 3 countries.

Bálint SzederInstitute of Enzymology, Research Centre for Natural Sciences, Hungarian Academy of Sciences, 1117 Budapest, Hungary. szeder.balint@ttk.mta.hu.
Júlia Tárnoki-ZáchDepartment of Biological Physics, Eötvös University, 1117 Budapest, Hungary. zachjuli@yahoo.fr.
Dóra LakatosDepartment of Biological Physics, Eötvös University, 1117 Budapest, Hungary. burek43@gmail.com.
Virág VasInstitute of Enzymology, Research Centre for Natural Sciences, Hungarian Academy of Sciences, 1117 Budapest, Hungary. kudlik.gyongyi@ttk.mta.hu.
Gyöngyi KudlikInstitute of Enzymology, Research Centre for Natural Sciences, Hungarian Academy of Sciences, 1117 Budapest, Hungary. mero.balazs@ttk.mta.hu.
Balázs MerőInstitute of Enzymology, Research Centre for Natural Sciences, Hungarian Academy of Sciences, 1117 Budapest, Hungary. mero.balazs@ttk.mta.hu.
Kitti KoprivanaczInstitute of Enzymology, Research Centre for Natural Sciences, Hungarian Academy of Sciences, 1117 Budapest, Hungary. koprivanacz.kitti@ttk.mta.hu.
László BányaiInstitute of Enzymology, Research Centre for Natural Sciences, Hungarian Academy of Sciences, 1117 Budapest, Hungary. banyai.laszlo@ttk.mta.hu.
Lilla HámoriInstitute of Enzymology, Research Centre for Natural Sciences, Hungarian Academy of Sciences, 1117 Budapest, Hungary. hamori.lilla@ttk.mta.hu.
Gergely RónaDepartment of Biochemistry and Molecular Pharmacology, New York University School of Medicine, New York, NY 10016, USA. gergely.rona@nyumc.org.
András CzirókDepartment of Biological Physics, Eötvös University, 1117 Budapest, Hungary. aczirok@kumc.edu.
András FürediInstitute of Enzymology, Research Centre for Natural Sciences, Hungarian Academy of Sciences, 1117 Budapest, Hungary. andras.fueredi@meduniwien.ac.at.
And László BudayInstitute of Enzymology, Research Centre for Natural Sciences, Hungarian Academy of Sciences, 1117 Budapest, Hungary. buday.laszlo@ttk.mta.hu.
Institute of Molecular Life Sciences · HUEötvös Loránd University · HUNew York University · USSemmelweis University · HU

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Epithelial to mesenchymal transition (EMT) is a multipurpose process involved in wound healing, development, and certain pathological processes, such as metastasis formation. The Tks4 scaffold protein has been implicated in cancer progression; however, its role in oncogenesis is not well defined. In this study, the function of Tks4 was investigated in HCT116 colon cancer cells by knocking the protein out using the CRISPR/Cas9 system. Surprisingly, the absence of Tks4 induced significant changes in cell morphology, motility, adhesion and expression, and localization of E-cadherin, which are all considered as hallmarks of EMT. In agreement with these findings, the marked appearance of fibronectin, a marker of the mesenchymal phenotype, was also observed in Tks4-KO cells. Analysis of the expression of well-known EMT transcription factors revealed that Snail2 was strongly overexpressed in cells lacking Tks4. Tks4-KO cells showed increased motility and decreased cell-cell attachment. Collagen matrix invasion assays demonstrated the abundance of invasive solitary cells. Finally, the reintroduction of Tks4 protein in the Tks4-KO cells restored the expression levels of relevant key transcription factors, suggesting that the Tks4 scaffold protein has a specific and novel role in EMT regulation and cancer progression.

Indexed as

Adaptor Proteins, Signal TransducingCell MovementCell Transformation, NeoplasticColonic NeoplasmsEpithelial-Mesenchymal TransitionGene Expression Regulation, NeoplasticGene Knockout TechniquesHCT116 CellsHumansNeoplasm InvasivenessSignal TransductionAdaptor Proteins, Signal TransducingSH3PXD2B protein, humanEMTHCT116invasivenessmotilityscaffold proteinTks4

Identifiers

PMID31671862
PMCPMC6912613
OpenAlexW2982443518

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.