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@ARTICLE{Sanwald:877532,
      author       = {Sanwald, Julia L. and Poschmann, Gereon and Stühler, Kai
                      and Behrends, Christian and Hoffmann, Silke and Willbold,
                      Dieter},
      title        = {{T}he {GABARAP} {C}o-{S}ecretome {I}dentified by
                      {APEX}2-{GABARAP} {P}roximity {L}abelling of {E}xtracellular
                      {V}esicles},
      journal      = {Cells},
      volume       = {9},
      number       = {6},
      issn         = {2073-4409},
      address      = {Basel},
      publisher    = {MDPI},
      reportid     = {FZJ-2020-02268},
      pages        = {1468 -},
      year         = {2020},
      abstract     = {The autophagy-related ATG8 protein GABARAP has not only
                      been shown to be involved in the cellular self-degradation
                      process called autophagy but also fulfils functions in
                      intracellular trafficking processes such as receptor
                      transport to the plasma membrane. Notably, available mass
                      spectrometry data suggest that GABARAP is also secreted into
                      extracellular vesicles (EVs). Here, we confirm this finding
                      by the immunoblotting of EVs isolated from cell culture
                      supernatants and human blood serum using specific
                      anti-GABARAP antibodies. To investigate the mechanism by
                      which GABARAP is secreted, we applied proximity labelling, a
                      method for studying the direct environment of a protein of
                      interest in a confined cellular compartment. By expressing
                      an engineered peroxidase (APEX2)-tagged variant of
                      GABARAP—which, like endogenous GABARAP, was present in EVs
                      prepared from HEK293 cells—we demonstrate the
                      applicability of APEX2-based proximity labelling to EVs. The
                      biotinylated protein pool which contains the APEX2-GABARAP
                      co-secretome contained not only known GABARAP interaction
                      partners but also proteins that were found in
                      APEX2-GABARAP’s proximity inside of autophagosomes in an
                      independent study. All in all, we not only introduce a
                      versatile tool for co-secretome analysis in general but also
                      uncover the first details about autophagy-based pathways as
                      possible biogenesis mechanisms of GABARAP-containing EVs.},
      cin          = {IBI-7},
      ddc          = {570},
      cid          = {I:(DE-Juel1)IBI-7-20200312},
      pnm          = {552 - Engineering Cell Function (POF3-552)},
      pid          = {G:(DE-HGF)POF3-552},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:32560054},
      UT           = {WOS:000553607900001},
      doi          = {10.3390/cells9061468},
      url          = {https://juser.fz-juelich.de/record/877532},
}