Evidence map›Paper›PMID 23398121›Full record

ReviewEuropean journal of clinical investigation2013

Context-specific protein tyrosine kinase 6 (PTK6) signalling in prostate cancer.

Yu Zheng, Angela L Tyner

Open access · greenAbstract readReview
In one paragraph

Review in European journal of clinical investigation, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 32 papers.

0numbers the graph read from it
0cells of the map it votes in
32citing papers in PubMed
2.4field-weighted citation impact, top 12% 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

32 citing papers in PubMed, 42 citations in OpenAlex.

  1. Article
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  6. Bioinformatics-based prognostic value andFrontiers in oncology · 2025
    Article
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  9. Review
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  12. Review
  13. Article
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  15. Article
  16. Targeting protein tyrosine kinase 6 in cancer.Biochimica et biophysica acta. Reviews on cancer · 2020
    Review
  17. Protein tyrosine kinase 6 signaling in prostate cancer.American journal of clinical and experimental urology · 2020
    Review
  18. Article
  19. Vemurafenib Inhibits Active PTK6 inMolecular cancer therapeutics · 2019
    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

2 authors at 1 institution in 1 country.

Yu ZhengDepartment of Biochemistry and Molecular Genetics, University of Illinois at Chicago, Chicago, IL 60607, USA.
Angela L Tyner
University of Illinois Chicago · US

Funding

ISOLATION OF GENETIC MARKERS FOR INTESTINAL CRYPT CELLSR01DK044525 · NIDDK · UNIVERSITY OF ILLINOIS AT CHICAGO · PI TYNER, ANGELA L · 1993 to 2016
$4.8M
BRK/Sik Tyrosine Kinase Signaling in the ProstateR01DK068503 · NIDDK · UNIVERSITY OF ILLINOIS AT CHICAGO · PI TYNER, ANGELA L · 2005 to 2009
$1.4M
ISOLATION OF GENETIC MARKERS FOR INTESTINAL CRYPT CELLSR55DK044525 · NIDDK · UNIVERSITY OF ILLINOIS AT CHICAGO · PI TYNER, ANGELA L · 1992 to 1992
–
NIDDK NIH HHS DK44525NIDDK NIH HHS R01 DK044525NIDDK NIH HHS R01 DK068503
6 · The paper itself

Abstract

backgroundProtein tyrosine kinase 6 (PTK6) is an intracellular tyrosine kinase that is distantly related to SRC family kinases. PTK6 is nuclear in normal prostate epithelia, but nuclear localization is lost in prostate tumours. Increased expression of PTK6 is detected in human prostate cancer, especially at metastatic stages, and in other types of cancers, including breast, colon, head and neck cancers, and serous carcinoma of the ovary. MATERIALS AND

methodsPotential novel substrates of PTK6 identified by mass spectrometry were validated in vitro. The significance of PTK6-induced phosphorylation of these substrates was addressed using human prostate cell lines by knockdown of endogenous PTK6 or overexpression of targeted PTK6 to different intracellular compartments.

resultsWe identified AKT, p130CAS and focal adhesion kinase (FAK) as novel PTK6 substrates and demonstrated their roles in promoting cell proliferation, migration and resistance to anoikis. In prostate cancer cells, active PTK6 is primarily associated with membrane compartments, although the majority of total PTK6 is localized within the cytoplasm. Ectopic expression of membrane-targeted PTK6 transforms immortalized fibroblasts. Knockdown of endogenous cytoplasmic PTK6 in PC3 prostate cancer cells impairs proliferation, migration and anoikis resistance. However, re-introduction of PTK6 into the nucleus significantly decreases cell proliferation, suggesting context-specific functions for nuclear PTK6.

conclusionsIn human prostate cancer, elevated PTK6 expression, translocation of PTK6 from the nucleus to the cytoplasm and its activation at the plasma membrane contribute to increased phosphorylation and activation of its substrates such as AKT, p130CAS and FAK, thereby promoting prostate cancer progression.

Indexed as

Cell Line, TumorHumansMaleNeoplasm ProteinsProstatic NeoplasmsProtein-Tyrosine KinasesSignal TransductionNeoplasm ProteinsProtein-Tyrosine KinasesPTK6 protein, human

Identifiers

PMID23398121
PMCPMC3602132
OpenAlexW2064041964

What OpenQuestion holds

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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.