Evidence map›Paper›PMID 30145116›Full record

ArticleCell systems2018

Interdependence between EGFR and Phosphatases Spatially Established by Vesicular Dynamics Generates a Growth Factor Sensing and Responding Network.

Angel Stanoev, Amit Mhamane, Klaus C Schuermann, Hernán E Grecco, Wayne Stallaert, Martin Baumdick, Yannick Brüggemann, Maitreyi S Joshi, Pedro Roda-Navarro, Sven Fengler and 5 more

Open access · hybridAbstract read
In one paragraph

Article in Cell systems, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 32 papers.

0numbers the graph read from it
0cells of the map it votes in
32citing papers in PubMed
2.3field-weighted citation impact, top 11% 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

32 citing papers in PubMed, 53 citations in OpenAlex.

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  12. WNK1 controls endosomal trafficking through TRIM27-dependent regulation of actin assembly.Proceedings of the National Academy of Sciences of the United States of America · 2023
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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

15 authors at 2 institutions in 1 country.

Angel StanoevDepartment of Systemic Cell Biology, Max Planck Institute for Molecular Physiology, 44227 Dortmund, Germany.
Amit MhamaneDepartment of Systemic Cell Biology, Max Planck Institute for Molecular Physiology, 44227 Dortmund, Germany.
Klaus C SchuermannDepartment of Systemic Cell Biology, Max Planck Institute for Molecular Physiology, 44227 Dortmund, Germany.
Hernán E GreccoDepartment of Systemic Cell Biology, Max Planck Institute for Molecular Physiology, 44227 Dortmund, Germany.
Wayne StallaertDepartment of Systemic Cell Biology, Max Planck Institute for Molecular Physiology, 44227 Dortmund, Germany.
Martin BaumdickDepartment of Systemic Cell Biology, Max Planck Institute for Molecular Physiology, 44227 Dortmund, Germany.
Yannick BrüggemannDepartment of Systemic Cell Biology, Max Planck Institute for Molecular Physiology, 44227 Dortmund, Germany; Faculty of Chemistry and Chemical Biology, TU Dortmund, 44227 Dortmund, Germany.
Maitreyi S JoshiDepartment of Systemic Cell Biology, Max Planck Institute for Molecular Physiology, 44227 Dortmund, Germany.
Pedro Roda-NavarroDepartment of Systemic Cell Biology, Max Planck Institute for Molecular Physiology, 44227 Dortmund, Germany.
Sven FenglerDepartment of Systemic Cell Biology, Max Planck Institute for Molecular Physiology, 44227 Dortmund, Germany.
Rabea StockertDepartment of Systemic Cell Biology, Max Planck Institute for Molecular Physiology, 44227 Dortmund, Germany.
Lisaweta RoßmannekDepartment of Systemic Cell Biology, Max Planck Institute for Molecular Physiology, 44227 Dortmund, Germany.
Jutta LuigDepartment of Systemic Cell Biology, Max Planck Institute for Molecular Physiology, 44227 Dortmund, Germany.
Aneta KoseskaDepartment of Systemic Cell Biology, Max Planck Institute for Molecular Physiology, 44227 Dortmund, Germany; Faculty of Chemistry and Chemical Biology, TU Dortmund, 44227 Dortmund, Germany. Electronic address: aneta.koseska@mpi-dortmund.mpg.de.
Philippe I H BastiaensDepartment of Systemic Cell Biology, Max Planck Institute for Molecular Physiology, 44227 Dortmund, Germany; Faculty of Chemistry and Chemical Biology, TU Dortmund, 44227 Dortmund, Germany. Electronic address: philippe.bastiaens@mpi-dortmund.mpg.de.
Max Planck Institute of Molecular Physiology · DETU Dortmund University · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The proto-oncogenic epidermal growth factor receptor (EGFR) is a tyrosine kinase whose sensitivity to growth factors and signal duration determines cellular behavior. We resolve how EGFR's response to epidermal growth factor (EGF) originates from dynamically established recursive interactions with spatially organized protein tyrosine phosphatases (PTPs). Reciprocal genetic PTP perturbations enabled identification of receptor-like PTPRG/J at the plasma membrane and ER-associated PTPN2 as the major EGFR dephosphorylating activities. Imaging spatial-temporal PTP reactivity revealed that vesicular trafficking establishes a spatially distributed negative feedback with PTPN2 that determines signal duration. On the other hand, single-cell dose-response analysis uncovered a reactive oxygen species-mediated toggle switch between autocatalytically activated monomeric EGFR and the tumor suppressor PTPRG that governs EGFR's sensitivity to EGF. Vesicular recycling of monomeric EGFR unifies the interactions with these PTPs on distinct membrane systems, dynamically generating a network architecture that can sense and respond to time-varying growth factor signals.

Indexed as

Cell MembraneComputational BiologyCytoplasmic VesiclesEndoplasmic ReticulumEpidermal Growth FactorErbB ReceptorsFeedback, PhysiologicalHumansMCF-7 CellsMicroscopy, ConfocalModels, TheoreticalPhosphorylationProtein Interaction MapsProtein TransportProtein Tyrosine Phosphatase, Non-Receptor Type 2Reactive Oxygen SpeciesEGFR protein, humanEpidermal Growth FactorErbB ReceptorsProtein Tyrosine Phosphatase, Non-Receptor Type 2PTPN2 protein, humanReactive Oxygen SpeciesReceptor-Like Protein Tyrosine Phosphatases, Class 5RNA, Small Interferingautocatalysisdynamic organizationdynamic systems theoryEGFR phosphatome identificationfunctional imaginggrowth factor sensingin situ reactivity of phosphatasesquantifiable genetic perturbationsspatial-temporalvesicular trafficking

Identifiers

PMID30145116
PMCPMC6167251
OpenAlexW2888730537

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.