Evidence map›Paper›PMID 23095747›Full record

ArticleThe Journal of biological chemistry2012

Insights into ectodomain shedding and processing of protein-tyrosine pseudokinase 7 (PTK7).

Vladislav S Golubkov, Alex Y Strongin

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.

0numbers the graph read from it
0cells of the map it votes in
21citing papers in PubMed
1.7field-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

21 citing papers in PubMed, 32 citations in OpenAlex.

  1. Review
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  8. Matrix metalloproteinases - From the cleavage data to the prediction tools and beyond.Biochimica et biophysica acta. Molecular cell research · 2017
    Review
  9. Review
  10. Review
  11. Review
  12. Article
  13. Article
  14. Matrix metalloproteinases as breast cancer drivers and therapeutic targets.Frontiers in bioscience (Landmark edition) · 2015
    Review
  15. Article
  16. Article
  17. Article
  18. Article
  19. Article
  20. Receptor tyrosine kinases in the nucleus.Cold Spring Harbor perspectives in biology · 2013
    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

2 authors at 1 institution in 1 country.

Vladislav S GolubkovCancer Research Center, Sanford-Burnham Institute for Medical Research, La Jolla, California 92037, USA. vgolubkov@sanfordburnham.org
Alex Y Strongin
Sanford Burnham Prebys Medical Discovery Institute · US

Funding

METALLOPROTEINASES IN TUMOR NEOVASCULARIZATIONR01CA083017 · NCI · SANFORD BURNHAM PREBYS MEDICAL DISCOVERY INSTITUTE · PI STRONGIN, ALEX Y · 1999 to 2014
$3.8M
MT1-MMP pericellular proteolysis in malignancyR01CA077470 · NCI · SANFORD BURNHAM PREBYS MEDICAL DISCOVERY INSTITUTE · PI STRONGIN, ALEX Y · 1999 to 2009
$3.1M
Biochemistry of MT1-MMP activation in malignancyR01CA157328 · NCI · SANFORD BURNHAM PREBYS MEDICAL DISCOVERY INSTITUTE · PI STRONGIN, ALEX Y · 2011 to 2015
$1.9M
NCI NIH HHS CA157328NCI NIH HHS CA77470NCI NIH HHS CA83017NCI NIH HHS R01 CA077470NCI NIH HHS R01 CA083017NCI NIH HHS R01 CA157328
6 · The paper itself

Abstract

The membrane PTK7 pseudokinase, a component of both the canonical and noncanonical/planar cell polarity Wnt pathways, modulates cell polarity and motility in biological processes as diverse as embryo development and cancer cell invasion. To determine the individual proteolytic events and biological significance of the ectodomain shedding in the PTK7 function, we used highly invasive fibrosarcoma HT1080 cells as a model system. Current evidence suggested a likely link between PTK7 shedding and cell invasion in our HT1080 cell model system. We also demonstrated that in HT1080 cells the cleavage of the PTK7 ectodomain by an ADAM proteinase was coupled with the membrane type-1 matrix metalloproteinase (MT1-MMP) cleavage of the PKP(621)↓LI site in the seventh Ig-like domain of PTK7. Proteolytic cleavages led to the generation of two soluble, N-terminal and two matching C-terminal, cell-associated fragments of PTK7. This proteolysis was a prerequisite for the intramembrane cleavage of the C-terminal fragments of PTK7 by γ-secretase. γ-Secretase cleavage was predominantly followed by the efficient decay of the resulting C-terminal PTK7 fragment via the proteasome. In contrast, in HT1080 cells, which overexpressed the C-terminal PTK7 fragment, the latter readily entered the nucleus. Our data imply that therapeutic inhibition of PTK7 shedding may be used to slow cancer progression.

Indexed as

ProteolysisActive Transport, Cell NucleusADAM ProteinsAmyloid Precursor Protein SecretasesCell Adhesion MoleculesCell Line, TumorFibrosarcomaHumansMatrix Metalloproteinase 14Neoplasm InvasivenessProtein Structure, TertiaryReceptor Protein-Tyrosine KinasesSolubilityADAM ProteinsAmyloid Precursor Protein SecretasesCell Adhesion MoleculesMatrix Metalloproteinase 14PTK7 protein, humanReceptor Protein-Tyrosine Kinases

Identifiers

PMID23095747
PMCPMC3516747
OpenAlexW2039663245

What OpenQuestion holds

Textmetadata
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.