Evidence map›Paper›PMID 23792450›Full record

ArticleOncogene2014

Integrin α3β1-CD151 complex regulates dimerization of ErbB2 via RhoA.

V Novitskaya, H Romanska, R Kordek, P Potemski, R Kusińska, M Parsons, E Odintsova, F Berditchevski

Abstract read
PubMed Publisher
In one paragraph

Article in Oncogene, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.

0numbers the graph read from it
0cells of the map it votes in
24citing papers in PubMed
2.8field-weighted citation impact, top 10% 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

24 citing papers in PubMed, 60 citations in OpenAlex.

  1. CD151 interacts with integrin beta 2 in B cell lymphomas.Cellular and molecular life sciences : CMLS · 2025
    Article
  2. Review
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  7. Review
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  11. Article
  12. Review
  13. CD151 up-regulation contributes to the invasion of pituitary adenomas.International journal of clinical and experimental pathology · 2018
    Article
  14. Article
  15. Tetraspanins Function as Regulators of Cellular Signaling.Frontiers in cell and developmental biology · 2017
    Review
  16. Article
  17. Review
  18. Article
  19. 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

8 authors at 3 institutions in 2 countries.

V NovitskayaSchool of Cancer Sciences, The University of Birmingham, Edgbaston, Birmingham, UK.
H RomanskaDepartment of Pathology and Chemotherapy, Medical University of Łódź, Łódź, Poland.
R KordekDepartment of Pathology and Chemotherapy, Medical University of Łódź, Łódź, Poland.
P PotemskiDepartment of Pathology and Chemotherapy, Medical University of Łódź, Łódź, Poland.
R KusińskaDepartment of Pathology and Chemotherapy, Medical University of Łódź, Łódź, Poland.
M ParsonsRandall Division of Cell and Molecular Biophysics, King's College London, New Hunts House, Guys Campus, London, UK.
E OdintsovaSchool of Cancer Sciences, The University of Birmingham, Edgbaston, Birmingham, UK.
F BerditchevskiSchool of Cancer Sciences, The University of Birmingham, Edgbaston, Birmingham, UK.
Medical University of Lodz · PLUniversity of Birmingham · GBKing's College London · GB

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Integrin α3β1 regulates adhesive interactions of cells with laminins and have a critical role in adhesion-dependent cellular responses. Here, we examined the role of α3β1-integrin in ErbB2-dependent proliferation of breast cancer cells in three-dimensional laminin-rich extracellular matrix (3D lr-ECM). Depletion of α3β1 in ErbB2-overexpressing breast cancer cells suppressed growth and restore cell polarity in 3D lr-ECM. The phenotype of α3β1-depleted cells was reproduced upon depletion of tetraspanin CD151 and mirrored that of the cells treated with Herceptin, an established ErbB2 antagonist. Breast cancer cells expressing the α3β1-CD151 complex have higher steady-state phosphorylation of ErbB2 and show enhanced dimerization of the protein when compared with α3β1-/CD151-depleted cells. Furthermore, Herceptin-dependent dephosphorylation of ErbB2 was only observed in α3β1-CD151-expressing cells. Importantly, the inhibitory activity of Herceptin was more pronounced when cells expressed both α3β1 and CD151. We also found that the level of active RhoA was increased in α3β1- and CD151-depleted cells and that Rho controls dimerization of ErbB2. Expression of α3β1 alone did not have significant prognostic value in patients with invasive ductal carcinoma of the breast. However, expression of α3β1 in combination with CD151 represented a more stringent indicator of poor survival than CD151 alone. Taken together, these results demonstrate that the α3β1-CD151 complex has a critical regulatory role in ErbB2-dependent signalling and thereby may be involved in breast cancer progression.

Indexed as

Antibodies, Monoclonal, HumanizedAntineoplastic AgentsBreast NeoplasmsCell Line, TumorCell PolarityErb-b2 Receptor Tyrosine KinasesFemaleHumansIntegrin alpha3beta1PhosphorylationPrognosisProportional Hazards ModelsProtein MultimerizationProtein Processing, Post-TranslationalrhoA GTP-Binding ProteinSignal TransductionAntibodies, Monoclonal, HumanizedAntineoplastic AgentsCD151 protein, humanERBB2 protein, humanErb-b2 Receptor Tyrosine KinasesIntegrin alpha3beta1rhoA GTP-Binding ProteinRHOA protein, humanTetraspanin 24Trastuzumab

Identifiers

PMID23792450
OpenAlexW1993759825

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.