% IMPORTANT: The following is UTF-8 encoded.  This means that in the presence
% of non-ASCII characters, it will not work with BibTeX 0.99 or older.
% Instead, you should use an up-to-date BibTeX implementation like “bibtex8” or
% “biber”.

@ARTICLE{Stanoev:140235,
      author       = {Stanoev, Angel and Mhamane, Amit and Schuermann, Klaus C
                      and Grecco, Hernán E and Stallaert, Wayne and Baumdick,
                      Martin and Brüggemann, Yannick and Joshi, Maitreyi S and
                      Roda-Navarro, Pedro and Fengler, Sven and Stockert, Rabea
                      and Roßmannek, Lisaweta and Luig, Jutta and Koseska, Aneta
                      and Bastiaens, Philippe I H},
      title        = {{I}nterdependence between {EGFR} and {P}hosphatases
                      {S}patially {E}stablished by {V}esicular {D}ynamics
                      {G}enerates a {G}rowth {F}actor {S}ensing and {R}esponding
                      {N}etwork.},
      journal      = {Cell systems},
      volume       = {7},
      number       = {3},
      issn         = {2405-4712},
      address      = {Maryland Heights, MO},
      publisher    = {Elsevier},
      reportid     = {DZNE-2020-06557},
      pages        = {295-309.e11},
      year         = {2018},
      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.},
      keywords     = {Cell Membrane: metabolism / Computational Biology /
                      Cytoplasmic Vesicles: metabolism / Endoplasmic Reticulum:
                      metabolism / Epidermal Growth Factor: metabolism / ErbB
                      Receptors: metabolism / Feedback, Physiological / Humans /
                      MCF-7 Cells / Microscopy, Confocal / Models, Theoretical /
                      Phosphorylation / Protein Interaction Maps / Protein
                      Transport / Protein Tyrosine Phosphatase, Non-Receptor Type
                      2: metabolism / RNA, Small Interfering: genetics / Reactive
                      Oxygen Species: metabolism / Receptor-Like Protein Tyrosine
                      Phosphatases, Class 5: genetics / Receptor-Like Protein
                      Tyrosine Phosphatases, Class 5: metabolism / Signal
                      Transduction / Single-Cell Analysis / RNA, Small Interfering
                      (NLM Chemicals) / Reactive Oxygen Species (NLM Chemicals) /
                      Epidermal Growth Factor (NLM Chemicals) / EGFR protein,
                      human (NLM Chemicals) / ErbB Receptors (NLM Chemicals) /
                      PTPN2 protein, human (NLM Chemicals) / Protein Tyrosine
                      Phosphatase, Non-Receptor Type 2 (NLM Chemicals) /
                      Receptor-Like Protein Tyrosine Phosphatases, Class 5 (NLM
                      Chemicals)},
      cin          = {AG Fava 1},
      ddc          = {570},
      cid          = {I:(DE-2719)1013016},
      pnm          = {342 - Disease Mechanisms and Model Systems (POF3-342)},
      pid          = {G:(DE-HGF)POF3-342},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:30145116},
      pmc          = {pmc:PMC6167251},
      doi          = {10.1016/j.cels.2018.06.006},
      url          = {https://pub.dzne.de/record/140235},
}