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@ARTICLE{Sanwald:889879,
      author       = {Sanwald, Julia L. and Dobner, Jochen and Simons, Indra M.
                      and Poschmann, Gereon and Stühler, Kai and Üffing, Alina
                      and Hoffmann, Silke and Willbold, Dieter},
      title        = {{L}ack of {GABARAP}-{T}ype {P}roteins {I}s {A}ccompanied by
                      {A}ltered {G}olgi {M}orphology and {S}urfaceome
                      {C}omposition},
      journal      = {International journal of molecular sciences},
      volume       = {22},
      number       = {1},
      issn         = {1422-0067},
      address      = {Basel},
      publisher    = {Molecular Diversity Preservation International},
      reportid     = {FZJ-2021-00487},
      pages        = {85 -},
      year         = {2021},
      abstract     = {GABARAP (γ-aminobutyric acid type A receptor-associated
                      protein) and its paralogues GABARAPL1 and GABARAPL2 comprise
                      a subfamily of autophagy-related Atg8 proteins. They are
                      studied extensively regarding their roles during autophagy.
                      Originally, however, especially GABARAPL2 was discovered to
                      be involved in intra-Golgi transport and homotypic fusion of
                      post-mitotic Golgi fragments. Recently, a broader function
                      of mammalian Atg8s on membrane trafficking through
                      interaction with various soluble N-ethylmaleimide-sensitive
                      factor-attachment protein receptors SNAREs was suggested. By
                      immunostaining and microscopic analysis of the Golgi
                      network, we demonstrate the importance of the presence of
                      individual GABARAP-type proteins on Golgi morphology.
                      Furthermore, triple knockout (TKO) cells lacking the whole
                      GABARAP subfamily showed impaired Golgi-dependent vesicular
                      trafficking as assessed by imaging of fluorescently labelled
                      ceramide. With the Golgi apparatus being central within the
                      secretory pathway, we sought to investigate the role of the
                      GABARAP-type proteins for cell surface protein trafficking.
                      By analysing the surfaceome compositionofTKOs, we identified
                      a subset of cell surface proteins with altered plasma
                      membrane localisation. Taken together, we provide novel
                      insights into an underrated aspect of autophagy-independent
                      functions of the GABARAP subfamily and recommend considering
                      the potential impact of GABARAP subfamily proteins on a
                      plethora of processes during experimental analysis of
                      GABARAP-deficient cells not only in the autophagic context.},
      cin          = {IBI-7},
      ddc          = {540},
      cid          = {I:(DE-Juel1)IBI-7-20200312},
      pnm          = {5241 - Molecular Information Processing in Cellular Systems
                      (POF4-524)},
      pid          = {G:(DE-HGF)POF4-5241},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {33374830},
      UT           = {WOS:000606050100001},
      doi          = {10.3390/ijms22010085},
      url          = {https://juser.fz-juelich.de/record/889879},
}