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@ARTICLE{Viegas:866585,
      author       = {Viegas, Aldino and Yin, Dongsheng M. and Borggräfe, Jan
                      and Viennet, Thibault and Falke, Marcel and Schmitz, Anton
                      and Famulok, Michael and Etzkorn, Manuel},
      title        = {{M}olecular {A}rchitecture of a {N}etwork of {P}otential
                      {I}ntracellular {EGFR} {M}odulators {I}nvolving the
                      {J}uxtamembrane {S}egment, {ARNO}, {P}hospholipids and
                      {C}a{M}},
      journal      = {Structure},
      volume       = {28},
      issn         = {0969-2126},
      address      = {Cambridge, Mass.},
      publisher    = {Cell Press},
      reportid     = {FZJ-2019-05668},
      pages        = {54-62},
      year         = {2020},
      abstract     = {Signaling of the Epidermal growth factor receptors (EGFRs)
                      is a central cellular element and its dysregulation is
                      related to a number of severe diseases. While ligand binding
                      to the extracellular domain is the receptor’s most obvious
                      regulatory element, also intracellular factors can act as
                      modulators of EGFR activity. The juxtamembrane (JM) segment
                      of the EGFR seems to be a key interaction interface of these
                      cytoplasmic factors. However, very few JM-interacting
                      molecules have been identified so far and even fewer is
                      known about the molecular mechanism underlying JM-targeted
                      receptor modulation. Here we report ARNO as a new EGFR-JM
                      binding protein and provide high-resolution insights into
                      its mode of interaction. We obtain comparable insights also
                      for the known interaction partners Calmodulin and
                      phospholipid bilayers containing different lipid
                      compositions. Our results show clear similarities and
                      distinct differences in each binding mode. Furthermore, we
                      show that each interaction can be modulated by a set of
                      additional orthogonal factors generating a distinctly
                      regulated competitive network of possible EGFR modulators
                      acting on the intracellular domain of the receptor. This
                      newly identified interaction network and the obtained
                      insights into the underlaying molecular mechanism may foster
                      future EGFR-targeted therapeutic strategies.},
      cin          = {ICS-6},
      ddc          = {540},
      cid          = {I:(DE-Juel1)ICS-6-20110106},
      pnm          = {552 - Engineering Cell Function (POF3-552)},
      pid          = {G:(DE-HGF)POF3-552},
      typ          = {PUB:(DE-HGF)16},
      doi          = {10.2139/ssrn.3441425},
      url          = {https://juser.fz-juelich.de/record/866585},
}