Evidence map›Paper›PMID 25263444›Full record

ArticleOncogene2015

Protein tyrosine phosphatase PTPN3 inhibits lung cancer cell proliferation and migration by promoting EGFR endocytic degradation.

M-Y Li, P-L Lai, Y-T Chou, A-P Chi, Y-Z Mi, K-H Khoo, G-D Chang, C-W Wu, T-C Meng, G-C Chen

Abstract read
PubMed Publisher
In one paragraph

Article in Oncogene, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.

0numbers the graph read from it
0cells of the map it votes in
26citing 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

26 citing papers in PubMed.

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  18. High Expression of PTPN3 Predicts Progression and Unfavorable Prognosis of Glioblastoma.Medical science monitor : international medical journal of experimental and clinical research · 2018
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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

10 authors.

M-Y Li1] Institute of Biological Chemistry, Academia Sinica, Taipei, Taiwan [2] Institute of Biochemical Sciences, College of Life Science, National Taiwan University, Taipei, Taiwan.
P-L LaiInstitute of Biological Chemistry, Academia Sinica, Taipei, Taiwan.
Y-T ChouInstitute of Biomedical Sciences, Academia Sinica, Taipei, Taiwan.
A-P ChiInstitute of Biological Chemistry, Academia Sinica, Taipei, Taiwan.
Y-Z MiInstitute of Biological Chemistry, Academia Sinica, Taipei, Taiwan.
K-H Khoo1] Institute of Biological Chemistry, Academia Sinica, Taipei, Taiwan [2] Institute of Biochemical Sciences, College of Life Science, National Taiwan University, Taipei, Taiwan.
G-D ChangInstitute of Biochemical Sciences, College of Life Science, National Taiwan University, Taipei, Taiwan.
C-W WuInstitute of Biomedical Sciences, Academia Sinica, Taipei, Taiwan.
T-C Meng1] Institute of Biological Chemistry, Academia Sinica, Taipei, Taiwan [2] Institute of Biochemical Sciences, College of Life Science, National Taiwan University, Taipei, Taiwan.
G-C Chen1] Institute of Biological Chemistry, Academia Sinica, Taipei, Taiwan [2] Institute of Biochemical Sciences, College of Life Science, National Taiwan University, Taipei, Taiwan.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Epidermal growth factor receptor (EGFR) regulates multiple signaling cascades essential for cell proliferation, growth and differentiation. Using a genetic approach, we found that Drosophila FERM and PDZ domain-containing protein tyrosine phosphatase, dPtpmeg, negatively regulates border cell migration and inhibits the EGFR/Ras/mitogen-activated protein kinase signaling pathway during wing morphogenesis. We further identified EGFR pathway substrate 15 (Eps15) as a target of dPtpmeg and its human homolog PTPN3. Eps15 is a scaffolding adaptor protein known to be involved in EGFR endocytosis and trafficking. Interestingly, PTPN3-mediated tyrosine dephosphorylation of Eps15 promotes EGFR for lipid raft-mediated endocytosis and lysosomal degradation. PTPN3 and the Eps15 tyrosine phosphorylation-deficient mutant suppress non-small-cell lung cancer cell growth and migration in vitro and reduce lung tumor xenograft growth in vivo. Moreover, depletion of PTPN3 impairs the degradation of EGFR and enhances proliferation and tumorigenicity of lung cancer cells. Taken together, these results indicate that PTPN3 may act as a tumor suppressor in lung cancer through its modulation of EGFR signaling.

Indexed as

Cell MovementCell ProliferationAdaptor Proteins, Signal TransducingAnimalsAnimals, Genetically ModifiedCarcinoma, Non-Small-Cell LungCell LineCell Line, TumorEndocytosisErbB ReceptorsFemaleHEK293 CellsHumansImmunoblottingLung NeoplasmsMaleAdaptor Proteins, Signal TransducingEPS15 protein, humanErbB ReceptorsProtein Tyrosine Phosphatase, Non-Receptor Type 3PTPN3 protein, human

Identifiers

PMID25263444

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.