Evidence map›Paper›PMID 23924390›Full record

ArticleJournal of molecular signaling2013

EGF regulates tyrosine phosphorylation and membrane-translocation of the scaffold protein Tks5.

Anna Fekete, Gábor Bőgel, Szabolcs Pesti, Zalán Péterfi, Miklós Geiszt, László Buday

Abstract read
In one paragraph

Article in Journal of molecular signaling, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.

0numbers the graph read from it
0cells of the map it votes in
12citing papers in PubMed
–field-weighted citation impact
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

12 citing papers in PubMed.

  1. Article
  2. Article
  3. The Role of TKS5 in Chromosome Stability and Bladder Cancer Progression.International journal of molecular sciences · 2022
    Article
  4. Review
  5. Tks adaptor proteins at a glance.Journal of cell science · 2018
    Review
  6. Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Review
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.

Anna FeketeInstitute of Enzymology, Research Center for Natural Sciences, Hungarian Academy of Sciences, Budapest 1113, Hungary.
Gábor BőgelDepartment of Medical Chemistry, Semmelweis University Medical School, Budapest 1094, Hungary.
Szabolcs PestiDepartment of Medical Chemistry, Semmelweis University Medical School, Budapest 1094, Hungary.
Zalán PéterfiDepartment of Physiology, Semmelweis University Medical School, Budapest, Hungary.
Miklós GeisztDepartment of Physiology, Semmelweis University Medical School, Budapest, Hungary ; "Lendület" Peroxidase Enzyme Research Group of the Semmelweis University and the Hungarian Academy of Sciences, Budapest 1094, Hungary.
László BudayInstitute of Enzymology, Research Center for Natural Sciences, Hungarian Academy of Sciences, Budapest 1113, Hungary ; Department of Medical Chemistry, Semmelweis University Medical School, Budapest 1094, Hungary.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

backgroundTks5/FISH is a scaffold protein comprising of five SH3 domains and one PX domain. Tks5 is a substrate of the tyrosine kinase Src and is required for the organization of podosomes/invadopodia implicated in invasion of tumor cells. Recent data have suggested that a close homologue of Tks5, Tks4, is implicated in the EGF signaling.

resultsHere, we report that Tks5 is a component of the EGF signaling pathway. In EGF-treated cells, Tks5 is tyrosine phosphorylated within minutes and the level of phosphorylation is sustained for at least 2 hours. Using specific kinase inhibitors, we demonstrate that tyrosine phosphorylation of Tks5 is catalyzed by Src tyrosine kinase. We show that treatment of cells with EGF results in plasma membrane translocation of Tks5. In addition, treatment of cells with LY294002, an inhibitor of PI 3-kinase, or mutation of the PX domain reduces tyrosine phosphorylation and membrane translocation of Tks5.

conclusionsOur results identify Tks5 as a novel component of the EGF signaling pathway.

Indexed as

EGF receptorPI 3-kinasePX domainSrcTks4Tks5

Identifiers

PMID23924390
PMCPMC3765130

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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.