Evidence map›Paper›PMID 33143131›Full record

ReviewInternational journal of molecular sciences2020

Advances in Understanding TKS4 and TKS5: Molecular Scaffolds Regulating Cellular Processes from Podosome and Invadopodium Formation to Differentiation and Tissue Homeostasis.

Gyöngyi Kudlik, Tamás Takács, László Radnai, Anita Kurilla, Bálint Szeder, Kitti Koprivanacz, Balázs L Merő, László Buday, Virag Vas

Open access · goldAbstract readReview
In one paragraph

Review in International journal of molecular sciences, 2020. 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
1.8field-weighted citation impact, top 16% 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, 39 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Analysis of Human miRNA Derived From Bladder Epithelial Cells Infected With Uropathogenic Escherichia coli.APMIS : acta pathologica, microbiologica, et immunologica Scandinavica · 2026
    Article
  5. Article
  6. Review
  7. Podosomes and Mechanical Force.Results and problems in cell differentiation · 2026
    Review
  8. Article
  9. Review
  10. Article
  11. Review
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Article
  20. Article
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.

Gyöngyi KudlikInstitute of Enzymology, Research Centre for Natural Sciences, 1117 Budapest, Hungary.
Tamás TakácsInstitute of Enzymology, Research Centre for Natural Sciences, 1117 Budapest, Hungary.
László RadnaiInstitute of Enzymology, Research Centre for Natural Sciences, 1117 Budapest, Hungary.ORCID 0000-0001-6843-3740
Anita KurillaInstitute of Enzymology, Research Centre for Natural Sciences, 1117 Budapest, Hungary.
Bálint SzederInstitute of Enzymology, Research Centre for Natural Sciences, 1117 Budapest, Hungary.
Kitti KoprivanaczInstitute of Enzymology, Research Centre for Natural Sciences, 1117 Budapest, Hungary.
Balázs L MerőInstitute of Enzymology, Research Centre for Natural Sciences, 1117 Budapest, Hungary.
László BudayInstitute of Enzymology, Research Centre for Natural Sciences, 1117 Budapest, Hungary.ORCID 0000-0003-3518-5757
Virag VasInstitute of Enzymology, Research Centre for Natural Sciences, 1117 Budapest, Hungary.
Institute of Molecular Life Sciences · HUScripps Research Institute · USSemmelweis University · HU

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Scaffold proteins are typically thought of as multi-domain "bridging molecules." They serve as crucial regulators of key signaling events by simultaneously binding multiple participants involved in specific signaling pathways. In the case of epidermal growth factor (EGF)-epidermal growth factor receptor (EGFR) binding, the activated EGFR contacts cytosolic SRC tyrosine-kinase, which then becomes activated. This process leads to the phosphorylation of SRC-substrates, including the tyrosine kinase substrates (TKS) scaffold proteins. The TKS proteins serve as a platform for the recruitment of key players in EGFR signal transduction, promoting cell spreading and migration. The TKS4 and the TKS5 scaffold proteins are tyrosine kinase substrates with four or five SH3 domains, respectively. Their structural features allow them to recruit and bind a variety of signaling proteins and to anchor them to the cytoplasmic surface of the cell membrane. Until recently, TKS4 and TKS5 had been recognized for their involvement in cellular motility, reactive oxygen species-dependent processes, and embryonic development, among others. However, a number of novel functions have been discovered for these molecules in recent years. In this review, we attempt to cover the diverse nature of the TKS molecules by discussing their structure, regulation by SRC kinase, relevant signaling pathways, and interaction partners, as well as their involvement in cellular processes, including migration, invasion, differentiation, and adipose tissue and bone homeostasis. We also describe related pathologies and the established mouse models.

Indexed as

Cell DifferentiationCell MovementHomeostasisAdaptor Proteins, Signal TransducingAdaptor Proteins, Vesicular TransportHumansPodosomesSignal TransductionAdaptor Proteins, Signal TransducingAdaptor Proteins, Vesicular TransportSH3PXD2A protein, humanSH3PXD2B protein, humanadipose tissuebone homeostasisepithelial–mesenchymal transitioninvasionmesenchymal stem cellsscaffold proteinTKS4TKS5tyrosine kinase substrates

Identifiers

PMID33143131
PMCPMC7663256
OpenAlexW3095828640

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.