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@ARTICLE{Btepage:857531,
      author       = {Bütepage, Mareike and Preisinger, Christian and von
                      Kriegsheim, Alexander and Scheufen, Anja and Lausberg, Eva
                      and Li, Jinyu and Kappes, Ferdinand and Feederle, Regina and
                      Ernst, Sabrina and Eckei, Laura and Krieg, Sarah and
                      Müller-Newen, Gerhard and Rossetti, Giulia and Feijs, Karla
                      L. H. and Verheugd, Patricia and Lüscher, Bernhard},
      title        = {{N}ucleolar-nucleoplasmic shuttling of {TARG}1 and its
                      control by {DNA} damage-induced poly-{ADP}-ribosylation and
                      by nucleolar transcription},
      journal      = {Scientific reports},
      volume       = {8},
      number       = {1},
      issn         = {2045-2322},
      address      = {[London]},
      publisher    = {Macmillan Publishers Limited, part of Springer Nature},
      reportid     = {FZJ-2018-06522},
      pages        = {6748},
      year         = {2018},
      abstract     = {Macrodomains are conserved protein folds associated with
                      ADP-ribose binding and turnover. ADP-ribosylation is a
                      posttranslational modification catalyzed primarily by ARTD
                      (aka PARP) enzymes in cells. ARTDs transfer either single or
                      multiple ADP-ribose units to substrates, resulting in mono-
                      or poly-ADP-ribosylation. TARG1/C6orf130 is a macrodomain
                      protein that hydrolyzes mono-ADP-ribosylation and interacts
                      with poly-ADP-ribose chains. Interactome analyses revealed
                      that TARG1 binds strongly to ribosomes and proteins
                      associated with rRNA processing and ribosomal assembly
                      factors. TARG1 localized to transcriptionally active
                      nucleoli, which occurred independently of ADP-ribose
                      binding. TARG1 shuttled continuously between nucleoli and
                      nucleoplasm. In response to DNA damage, which activates
                      ARTD1/2 (PARP1/2) and promotes synthesis of poly-ADP-ribose
                      chains, TARG1 re-localized to the nucleoplasm. This was
                      dependent on the ability of TARG1 to bind to
                      poly-ADP-ribose. These findings are consistent with the
                      observed ability of TARG1 to competitively interact with RNA
                      and PAR chains. We propose a nucleolar role of TARG1 in
                      ribosome assembly or quality control that is stalled when
                      TARG1 is re-located to sites of DNA damage.},
      cin          = {IAS-5 / JSC},
      ddc          = {600},
      cid          = {I:(DE-Juel1)IAS-5-20120330 / I:(DE-Juel1)JSC-20090406},
      pnm          = {574 - Theory, modelling and simulation (POF3-574) / 511 -
                      Computational Science and Mathematical Methods (POF3-511)},
      pid          = {G:(DE-HGF)POF3-574 / G:(DE-HGF)POF3-511},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:29712969},
      UT           = {WOS:000431107100007},
      doi          = {10.1038/s41598-018-25137-w},
      url          = {https://juser.fz-juelich.de/record/857531},
}