Evidence map›Paper›PMID 21376233›Full record

ArticleCell2011

Activation of multiple proto-oncogenic tyrosine kinases in breast cancer via loss of the PTPN12 phosphatase.

Tingting Sun, Nicola Aceto, Kristen L Meerbrey, Jessica D Kessler, Chunshui Zhou, Ilenia Migliaccio, Don X Nguyen, Natalya N Pavlova, Maria Botero, Jian Huang and 18 more

Open access · bronzeAbstract read
In one paragraph

Article in Cell, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 167 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
167citing papers in PubMed, 1 pooled it
13.8field-weighted citation impact, top 1% 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

167 citing papers in PubMed, 1 synthesis or guideline pooled it, 274 citations in OpenAlex.

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107 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

28 authors at 5 institutions in 2 countries.

Tingting SunVerna & Marrs McLean Department of Biochemistry & Molecular Biology, Baylor College of Medicine, One Baylor Plaza, Houston, TX 77030, USA.
Nicola Aceto
Kristen L Meerbrey
Jessica D Kessler
Chunshui Zhou
Ilenia Migliaccio
Don X Nguyen
Natalya N Pavlova
Maria Botero
Jian Huang
Ronald J Bernardi
Earlene Schmitt
Guang Hu
Mamie Z Li
Noah Dephoure
Steven P Gygi
Mitchell Rao
Chad J Creighton
Susan G Hilsenbeck
Chad A Shaw
Donna Muzny
Richard A Gibbs
David A Wheeler
C Kent Osborne
Rachel Schiff
Mohamed Bentires-Alj
Stephen J Elledge
Thomas F Westbrook
Baylor College of Medicine · USBrigham and Women's Hospital · USFriedrich Miescher Institute · CHHarvard University · USYale University · US

Funding

Tumor BiologyP30CA125123 · NCI · BAYLOR COLLEGE OF MEDICINE · PI DAVID R ROWLEY · 2007 to 2026
$73.9M
Role of Pluripotency Factors in Pluripotent Stem Cells, Development and DiseaseZIAES102745 · NIEHS · NATIONAL INSTITUTE OF ENVIRONMENTAL HEALTH SCIENCES · PI HU, GUANG · 2010 to 2025
$31.5M
TUMOR SUPPRESSOR GENES IN BREAST CANCER DEVELOPMENTP50CA058183 · NCI · UNIVERSITY OF TEXAS HLTH SCI CTR SAN ANT · PI OSBORNE, C KENT · 1992 to 2012
$30.9M
New Technologies for Quantitative Phosphorylation AnalysisR01HG003456 · NHGRI · HARVARD UNIVERSITY (MEDICAL SCHOOL) · PI GYGI, STEVEN P · 2005 to 2011
$2.7M
Howard Hughes Medical InstituteNCI NIH HHS P30 CA125123NCI NIH HHS P50 CA058183NHGRI NIH HHS HG3456NHGRI NIH HHS R01 HG003456
6 · The paper itself

Abstract

Among breast cancers, triple-negative breast cancer (TNBC) is the most poorly understood and is refractory to current targeted therapies. Using a genetic screen, we identify the PTPN12 tyrosine phosphatase as a tumor suppressor in TNBC. PTPN12 potently suppresses mammary epithelial cell proliferation and transformation. PTPN12 is frequently compromised in human TNBCs, and we identify an upstream tumor-suppressor network that posttranscriptionally controls PTPN12. PTPN12 suppresses transformation by interacting with and inhibiting multiple oncogenic tyrosine kinases, including HER2 and EGFR. The tumorigenic and metastatic potential of PTPN12-deficient TNBC cells is severely impaired upon restoration of PTPN12 function or combined inhibition of PTPN12-regulated tyrosine kinases, suggesting that TNBCs are dependent on the proto-oncogenic tyrosine kinases constrained by PTPN12. Collectively, these data identify PTPN12 as a commonly inactivated tumor suppressor and provide a rationale for combinatorially targeting proto-oncogenic tyrosine kinases in TNBC and other cancers based on their profile of tyrosine-phosphatase activity.

Indexed as

Breast NeoplasmsCell Line, TumorCell Transformation, NeoplasticErbB ReceptorsFemaleGene Expression Regulation, NeoplasticHumansMAP Kinase Signaling SystemMicroRNAsMutationNeoplasm MetastasisProtein Processing, Post-TranslationalProtein Tyrosine Phosphatase, Non-Receptor Type 12Tumor Suppressor ProteinsEGFR protein, humanErbB ReceptorsMicroRNAsMIRN124 microRNA, humanProtein Tyrosine Phosphatase, Non-Receptor Type 12PTPN12 protein, humanTumor Suppressor Proteins

Identifiers

PMID21376233
PMCPMC6014607
OpenAlexW2122858192

What OpenQuestion holds

Textmetadata
LicenceTDM
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.