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@ARTICLE{Ismail:172163,
      author       = {Ismail, Shehab A and Chen, Yong-Xiang and Rusinova,
                      Alexandra and Chandra, Anchal and Bierbaum, Martin and
                      Gremer, Lothar and Triola, Gemma and Waldmann, Herbert and
                      Bastiaens, Philippe I H and Wittinghofer, Alfred},
      title        = {{A}rl2-{GTP} and {A}rl3-{GTP} regulate a {GDI}-like
                      transport system for farnesylated cargo},
      journal      = {Nature chemical biology},
      volume       = {7},
      number       = {12},
      issn         = {1552-4469},
      address      = {Basingstoke},
      publisher    = {Nature Publishing Group},
      reportid     = {FZJ-2014-05673},
      pages        = {942 - 949},
      year         = {2011},
      abstract     = {Lipidated Rho and Rab GTP-binding proteins are transported
                      between membranes in complex with solubilizing factors
                      called ‘guanine nucleotide dissociation inhibitors’
                      (GDIs). Unloading from GDIs using GDI displacement factors
                      (GDFs) has been proposed but remains mechanistically
                      elusive. PDEd is a putative solubilizing factor for several
                      prenylated Ras-subfamily proteins. Here we report the
                      structure of fully modified farnesylated Rheb-GDP in complex
                      with PDEd. The structure explains the nucleotide-independent
                      binding of Rheb to PDEd and the relaxed specificity of PDEd.
                      We demonstrate that the G proteins Arl2 and Arl3 act in a
                      GTP-dependent manner as allosteric release factors for
                      farnesylated cargo. We thus describe a new transport system
                      for farnesylated G proteins involving a GDI-like molecule
                      and an unequivocal GDF. Considering the importance of PDEd
                      for proper Ras and Rheb signaling, this study is
                      instrumental in developing a new target for anticancer
                      therapy.},
      cin          = {ICS-6},
      ddc          = {540},
      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:000297166200018},
      pubmed       = {pmid:22002721},
      doi          = {10.1038/nchembio.686},
      url          = {https://juser.fz-juelich.de/record/172163},
}