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@ARTICLE{Dobner:875459,
      author       = {Dobner, Jochen and Simons, Indra M. and Rufinatscha,
                      Kerstin and Hänsch, Sebastian and Schwarten, Melanie and
                      Weiergräber, Oliver H. and Abdollahzadeh, Iman and Gensch,
                      Thomas and Bode, Johannes G. and Hoffmann, Silke and
                      Willbold, Dieter},
      title        = {{D}eficiency of {GABARAP} but not its {P}aralogs {C}auses
                      {E}nhanced {EGF}-induced {EGFR} {D}egradation},
      journal      = {Cells},
      volume       = {9},
      number       = {5},
      issn         = {2073-4409},
      address      = {Basel},
      publisher    = {MDPI},
      reportid     = {FZJ-2020-02051},
      pages        = {1296 -},
      year         = {2020},
      abstract     = {The γ-aminobutyric acid type A receptor-associated protein
                      (GABARAP) and its close paralogs GABARAPL1 and GABARAPL2
                      constitute a subfamily of the autophagy-related 8 (Atg8)
                      protein family. Being associated with a variety of dynamic
                      membranous structures of autophagic and non-autophagic
                      origin, Atg8 proteins functionalize membranes by either
                      serving as docking sites for other proteins or by acting as
                      membrane tethers or adhesion factors. In this study, we
                      describe that deficiency for GABARAP alone, but not for its
                      close paralogs, is sufficient for accelerated EGF receptor
                      (EGFR) degradation in response to EGF, which is accompanied
                      by the downregulation of EGFR-mediated MAPK signaling,
                      altered target gene expression, EGF uptake, and EGF vesicle
                      composition over time. We further show that GABARAP and EGFR
                      converge in the same distinct compartments at endogenous
                      GABARAP expression levels in response to EGF stimulation.
                      Furthermore, GABARAP associates with EGFR in living cells
                      and binds to synthetic peptides that are derived from the
                      EGFR cytoplasmic tail in vitro. Thus, our data strongly
                      indicate a unique and novel role for GABARAP during EGFR
                      trafficking.},
      cin          = {IBI-7},
      ddc          = {570},
      cid          = {I:(DE-Juel1)IBI-7-20200312},
      pnm          = {553 - Physical Basis of Diseases (POF3-553)},
      pid          = {G:(DE-HGF)POF3-553},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:32456010},
      UT           = {WOS:000539340200230},
      doi          = {10.3390/cells9051296},
      url          = {https://juser.fz-juelich.de/record/875459},
}