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@ARTICLE{ma:139650,
      author       = {ma, peixiang and Schwarten, M. and Schneider, L. and
                      Boeske, A. and Henke, N. and Lisak, D. and Weber, Stephan
                      and Mohrluder, J. and Stoldt, M. and Strodel, B. and
                      Methner, A. and Hoffmann, Silke and Weiergraber, O. H. and
                      Willbold, Dieter},
      title        = {{I}nteraction of {B}cl-2 with the autophagy-related {GABAA}
                      receptor-associated protein ({GABARAP}): biophysical
                      characterization and functional implications},
      journal      = {The journal of biological chemistry},
      volume       = {288},
      issn         = {1083-351X},
      address      = {Bethesda, Md.},
      publisher    = {jbc},
      reportid     = {FZJ-2013-05628},
      pages        = {37204-37215},
      year         = {2013},
      abstract     = {Apoptosis and autophagy are fundamental homeostatic
                      processes in eukaryotic organisms fulfilling essential roles
                      in development and adaptation. Recently, the anti-apoptotic
                      factor Bcl-2 has been reported to also inhibit autophagy,
                      thus establishing a potential link between these pathways,
                      but the mechanistic details are only beginning to emerge.
                      Here we show that Bcl-2 directly binds to the
                      phagophore-associated protein GABARAP. NMR experiments
                      revealed that the interaction critically depends on a
                      three-residue segment (EWD) of Bcl-2 adjacent to the BH4
                      region, which is anchored to one of the two hydrophobic
                      pockets on the GABARAP molecule. This is at variance with
                      the majority of GABARAP interaction partners identified
                      previously, which occupy both hydrophobic pockets
                      simultaneously. Bcl-2 affinity could also be detected for
                      GEC1, but not for other mammalian Atg8 homologs. Finally, we
                      provide evidence that overexpression of Bcl-2 inhibits
                      lipidation of GABARAP, a key step in autophagosome
                      formation, possibly via competition with the lipid
                      conjugation machinery. These results support the regulatory
                      role of Bcl-2 in autophagy and define GABARAP as a novel
                      interaction partner involved in this intricate connection.},
      cin          = {ICS-6},
      ddc          = {570},
      cid          = {I:(DE-Juel1)ICS-6-20110106},
      pnm          = {452 - Structural Biology (POF2-452)},
      pid          = {G:(DE-HGF)POF2-452},
      typ          = {PUB:(DE-HGF)16},
      UT           = {WOS:000329189700038},
      pubmed       = {pmid:24240096},
      doi          = {10.1074/jbc.M113.528067},
      url          = {https://juser.fz-juelich.de/record/139650},
}