Evidence map›Paper›PMID 31406243›Full record

ArticleOncogene2019

PTPN3 suppresses lung cancer cell invasiveness by counteracting Src-mediated DAAM1 activation and actin polymerization.

Meng-Yen Li, Wen-Hsin Peng, Chien-Hsun Wu, Ya-Min Chang, Yu-Ling Lin, Geen-Dong Chang, Han-Chung Wu, Guang-Chao Chen

Abstract read
PubMed Publisher
In one paragraph

Article in Oncogene, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing papers in PubMed
1.8field-weighted citation impact, top 14% 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

17 citing papers in PubMed, 33 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. The prognostic value of DAAM2 in lower grade glioma, liver cancer, and breast cancer.Clinical & translational oncology : official publication of the Federation of Spanish Oncology Societies and of the National Cancer Institute of Mexico · 2023
    Article
  6. Review
  7. Article
  8. Article
  9. Review
  10. Article
  11. Protein Tyrosine Phosphatases: Mechanisms in Cancer.International journal of molecular sciences · 2021
    Review
  12. Article
  13. Article
  14. Article
  15. Article
  16. Review
  17. 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

8 authors at 3 institutions in 1 country.

Meng-Yen LiInstitute of Biological Chemistry, Academia Sinica, Taipei, 115, Taiwan.
Wen-Hsin PengInstitute of Biological Chemistry, Academia Sinica, Taipei, 115, Taiwan.
Chien-Hsun WuInstitute of Cellular and Organismic Biology, Academia Sinica, Taipei, 115, Taiwan.
Ya-Min ChangInstitute of Biochemical Sciences, College of Life Science, National Taiwan University, Taipei, 106, Taiwan.
Yu-Ling LinInstitute of Biological Chemistry, Academia Sinica, Taipei, 115, Taiwan.
Geen-Dong ChangInstitute of Biochemical Sciences, College of Life Science, National Taiwan University, Taipei, 106, Taiwan.
Han-Chung WuInstitute of Cellular and Organismic Biology, Academia Sinica, Taipei, 115, Taiwan.
Guang-Chao ChenInstitute of Biological Chemistry, Academia Sinica, Taipei, 115, Taiwan. gcchen@gate.sinica.edu.tw.
Institute of Biological Chemistry, Academia Sinica · TWNational Taiwan University · TWInstitute of Cellular and Organismic Biology, Academia Sinica · TW

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Cancer cell migration plays a crucial role during the metastatic process. Reversible tyrosine phosphorylation by protein tyrosine kinases (PTKs) and protein tyrosine phosphatases (PTPs) have been implicated in the regulation of cancer cell migration and invasion. However, the underlying mechanisms have not been fully elucidated. Here, we show that depletion of the FERM and PDZ domain-containing protein tyrosine phosphatase PTPN3 enhances lung cancer cell migration/invasion and metastasis by promoting actin filament assembly and focal adhesion dynamics. We further identified Src and DAAM1 (dishevelled associated activator of morphogenesis 1) as interactors of PTPN3. DAAM1 is a formin-like protein involved in the regulation of actin cytoskeletal remodeling. PTPN3 inhibits Src activity and Src-mediated phosphorylation of Tyr652 on DAAM1. The tyrosine phosphorylation of DAAM1 is essential for DAAM1 homodimer formation and actin polymerization. Ectopic expression of a DAAM1 phosphodeficient mutant inhibited F-actin assembly and suppressed lung cancer cell migration and invasion. Our findings reveal a novel mechanism by which reversible tyrosine phosphorylation of DAAM1 by Src and PTPN3 regulates actin dynamics and lung cancer invasiveness.

Indexed as

Neoplasm InvasivenessActinsFocal AdhesionsHumansLung NeoplasmsMicrofilament ProteinsPolymerizationProtein Tyrosine Phosphatase, Non-Receptor Type 3Proto-Oncogene Proteins p21(ras)rho GTP-Binding ProteinsActinsDAAM1 protein, humanMicrofilament ProteinsProtein Tyrosine Phosphatase, Non-Receptor Type 3Proto-Oncogene Proteins p21(ras)PTPN3 protein, humanrho GTP-Binding Proteins

Identifiers

PMID31406243
OpenAlexW2968395735

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.