Evidence map›Paper›PMID 27956147›Full record

ArticleJournal of molecular biology2017

Systematic Identification of Oncogenic EGFR Interaction Partners.

Julia Petschnigg, Max Kotlyar, Louise Blair, Igor Jurisica, Igor Stagljar, Robin Ketteler

Open access · hybridAbstract read
In one paragraph

Article in Journal of molecular biology, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.

0numbers the graph read from it
0cells of the map it votes in
10citing papers in PubMed
1.7field-weighted citation impact, top 13% 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

10 citing papers in PubMed, 22 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. 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

6 authors at 4 institutions in 2 countries.

Julia PetschniggMRC Laboratory for Molecular Cell Biology, University College London, London, WC1E 6BT, UK.
Max KotlyarPrincess Margaret Cancer Center, University Health Network, Toronto, M5G 2M9, Canada.
Louise BlairMRC Laboratory for Molecular Cell Biology, University College London, London, WC1E 6BT, UK.
Igor JurisicaPrincess Margaret Cancer Center, University Health Network, Toronto, M5G 2M9, Canada; Department of Medical Biophysics, University of Toronto, Toronto, M5G 1L7, Canada; Department of Computer Science, University of Toronto, Toronto, M5S 2E4, Canada; TECHNA Institute for the Advancement of Technology for Health, Toronto, M5G 1L5, Canada.
Igor StagljarDonnelly Centre, Departments of Molecular Genetics and Biochemistry, University of Toronto, Toronto, M5S 3E1, Canada; Department of Molecular Genetics, University of Toronto, M5S 1A8, Canada; Department of Biochemistry, University of Toronto, M5S 1A8, Canada.
Robin KettelerMRC Laboratory for Molecular Cell Biology, University College London, London, WC1E 6BT, UK. Electronic address: r.ketteler@ucl.ac.uk.
MRC Laboratory for Molecular Cell Biology · GBOntario Institute for Cancer Research · CAUniversity Health Network · CAUniversity of Toronto · CA

Funding

BBSRC BB/JO/5881/1Medical Research Council MC_EX_G0800785
6 · The paper itself

Abstract

The epidermal growth factor receptor (EGFR) is a receptor tyrosine kinase (TK) that-once activated upon ligand binding-leads to receptor dimerization, recruitment of protein complexes, and activation of multiple signaling cascades. The EGFR is frequently overexpressed or mutated in various cancers leading to aberrant signaling and tumor growth. Hence, identification of interaction partners that bind to mutated EGFR can help identify novel targets for drug discovery. Here, we used a systematic approach to identify novel proteins that are involved in cancerous EGFR signaling. Using a combination of high-content imaging and a mammalian membrane two-hybrid protein-protein interaction method, we identified eight novel interaction partners of EGFR, of which half strongly interacted with oncogenic, hyperactive EGFR variants. One of these, transforming acidic coiled-coil proteins (TACC) 3, stabilizes EGFR on the cell surface, which results in an increase in downstream signaling via the mitogen-activated protein kinase and AKT pathway. Depletion of TACC3 from cells using small hairpin RNA (shRNA) knockdown or small-molecule targeting reduced mitogenic signaling in non-small cell lung cancer cell lines, suggesting that targeting TACC3 has potential as a new therapeutic approach for non-small cell lung cancer.

Indexed as

Gene Expression Regulation, NeoplasticCarcinoma, Non-Small-Cell LungCell SurvivalComputational BiologyErbB ReceptorsGene DeletionHEK293 CellsHeLa CellsHumansImmunoprecipitationMicrotubule-Associated ProteinsMitogen-Activated Protein KinasesPhosphorylationProtein Interaction Domains and MotifsRNA, Small InterferingSignal TransductionEGFR protein, humanErbB ReceptorsMicrotubule-Associated ProteinsMitogen-Activated Protein KinasesRNA, Small InterferingTACC3 protein, humanEGFRnon-small cell lung canceroncogenic signalingprotein–protein interactiontwo-hybrid screening

Identifiers

PMID27956147
PMCPMC5240790
OpenAlexW2560641415

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.