Evidence map›Paper›PMID 24217252›Full record

ArticleThe Journal of biological chemistry2013

Receptor protein-tyrosine phosphatase α regulates focal adhesion kinase phosphorylation and ErbB2 oncoprotein-mediated mammary epithelial cell motility.

Benoit Boivin, Fauzia Chaudhary, Bryan C Dickinson, Aftabul Haque, Stephanie C Pero, Christopher J Chang, Nicholas K Tonks

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.

0numbers the graph read from it
0cells of the map it votes in
15citing papers in PubMed
1.2field-weighted citation impact, top 21% 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

15 citing papers in PubMed, 19 citations in OpenAlex.

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  14. Review
  15. The HER2 Signaling Network in Breast Cancer--Like a Spider in its Web.Journal of mammary gland biology and neoplasia · 2014
    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

7 authors at 3 institutions in 1 country.

Benoit BoivinFrom the Cold Spring Harbor Laboratory, Cold Spring Harbor, New York 11724.
Fauzia Chaudhary
Bryan C Dickinson
Aftabul Haque
Stephanie C Pero
Christopher J Chang
Nicholas K Tonks
Cold Spring Harbor Laboratory · USHoward Hughes Medical Institute · USUniversity of Vermont · US

Funding

Single-Cell Biology Shared ResourceP30CA045508 · NCI · COLD SPRING HARBOR LABORATORY · PI John Edward Moses · 1987 to 2026
$118.9M
PROTEIN TYROSINE DEPHOSPHORYLATION &SIGNAL TRANSDUCTIONR01CA053840 · NCI · COLD SPRING HARBOR LABORATORY · PI TONKS, NICHOLAS K · 1991 to 2025
$11.8M
Molecular Imaging Probes To Study Redox BiologyR01GM079465 · NIGMS · UNIVERSITY OF CALIFORNIA BERKELEY · PI Christopher J. Chang · 2006 to 2026
$7.8M
Receptor PTPs, Cell Contract and Signal TransductionR01GM055989 · NIGMS · COLD SPRING HARBOR LABORATORY · PI TONKS, NICHOLAS K · 1997 to 2018
$6.7M
Protein Tyrosine Dephosphorylation &signal TransductionR37CA053840 · NCI · COLD SPRING HARBOR LABORATORY · PI TONKS, NICHOLAS K · 2001 to 2008
$5.2M
TARGETING BREAST CANCER WITH SMALL LIGANDSR01CA080790 · NCI · UNIVERSITY OF VERMONT &ST AGRIC COLLEGE · PI KRAG, DAVID N · 1999 to 2006
$1.5M
Howard Hughes Medical InstituteNCI NIH HHS CA45508NCI NIH HHS CA53840NCI NIH HHS P30 CA045508NCI NIH HHS R01 CA053840NCI NIH HHS R01 CA80790NCI NIH HHS R37 CA053840NIGMS NIH HHS GM55989NIGMS NIH HHS GM79465NIGMS NIH HHS R01 GM055989NIGMS NIH HHS R01 GM079465
6 · The paper itself

Abstract

We investigated the role of protein-tyrosine phosphatase α (PTPα) in regulating signaling by the ErbB2 oncoprotein in mammary epithelial cells. Using this model, we demonstrated that activation of ErbB2 led to the transient inactivation of PTPα, suggesting that attenuation of PTPα activity may contribute to enhanced ErbB2 signaling. Furthermore, RNAi-induced suppression of PTPα led to increased cell migration in an ErbB2-dependent manner. The ability of ErbB2 to increase cell motility in the absence of PTPα was characterized by prolonged interaction of GRB7 with ErbB2 and increased association of ErbB2 with a β1-integrin-rich complex, which depended on GRB7-SH2 domain interactions. Finally, suppression of PTPα resulted in increased phosphorylation of focal adhesion kinase on Tyr-407, which induced the recruitment of vinculin and the formation of a novel focal adhesion kinase complex in response to ErbB2 activation in mammary epithelial cells. Collectively, these results reveal a new role for PTPα in the regulation of motility of mammary epithelial cells in response to ErbB2 activation.

Indexed as

Cell LineCell MovementEpithelial CellsErb-b2 Receptor Tyrosine KinasesFocal Adhesion Kinase 1HumansMaleMammary Glands, HumanPhosphorylationReceptor-Like Protein Tyrosine Phosphatases, Class 4Signal TransductionVinculinERBB2 protein, humanErb-b2 Receptor Tyrosine KinasesFocal Adhesion Kinase 1PTK2 protein, humanPTPRA protein, humanReceptor-Like Protein Tyrosine Phosphatases, Class 4VCL protein, humanVinculinBreast CancerCell MotilityDephosphorylationErbB2FAKOncogenePhosphatasePhosphorylationProtein KinasesPTPα

Identifiers

PMID24217252
PMCPMC3873551
OpenAlexW2073807730

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.