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@INBOOK{Chang:857534,
      author       = {Bütepage, Mareike and Krieg, Sarah and Eckei, Laura and
                      Li, Jinyu and Rossetti, Giulia and Verheugd, Patricia and
                      Lüscher, Bernhard},
      editor       = {Chang, Paul},
      title        = {{A}ssessment of {I}ntracellular {A}uto-{M}odification
                      {L}evels of {ARTD}10 {U}sing
                      {M}ono-{ADP}-{R}ibose-{S}pecific {M}acrodomains 2 and 3 of
                      {M}urine {A}rtd8},
      volume       = {1813},
      address      = {New York, NY},
      publisher    = {Springer New York},
      reportid     = {FZJ-2018-06525},
      isbn         = {978-1-4939-8587-6 (print)},
      series       = {Methods in Molecular Biology},
      pages        = {41 - 63},
      year         = {2018},
      comment      = {ADP-ribosylation and NAD+ Utilizing Enzymes / Chang, Paul
                      (Editor) ; New York, NY : Springer New York, 2018, Chapter 4
                      ; ISSN: 1064-3745=1940-6029 ; ISBN:
                      978-1-4939-8587-6=978-1-4939-8588-3 ;
                      doi:10.1007/978-1-4939-8588-3},
      booktitle     = {ADP-ribosylation and NAD+ Utilizing
                       Enzymes / Chang, Paul (Editor) ; New
                       York, NY : Springer New York, 2018,
                       Chapter 4 ; ISSN: 1064-3745=1940-6029 ;
                       ISBN:
                       978-1-4939-8587-6=978-1-4939-8588-3 ;
                       doi:10.1007/978-1-4939-8588-3},
      abstract     = {Mono-ADP-ribosylation is a posttranslational modification,
                      which is catalyzed in cells by certain members of the
                      ADP-ribosyltransferase diphtheria toxin-like family (ARTD)
                      of ADP-ribosyltransferases (aka PARP enzymes). It involves
                      the transfer of a single residue of ADP-ribose (ADPr) from
                      the cofactor NAD+ onto substrate proteins. Although 12 of
                      the 17 members of the ARTD family have been defined as
                      mono-ARTDs in in vitro assays, relatively little is known
                      about their exact cellular functions. A major challenge is
                      the detection of mono-ADP-ribosylated (MARylated) proteins
                      in cells as no antibodies are available that detect
                      exclusively MARylated proteins. As an alternative to
                      classical antibodies, the MAR-specific binding domains
                      macro2 and macro3 of Artd8 can be utilized alone or in
                      combination, to demonstrate intracellular auto-modification
                      levels of ARTD10 in cells in both co-immunoprecipitation and
                      co-localization experiments. Here we demonstrate that
                      different macrodomain constructs of human ARTD8 and murine
                      Artd8, alone or in combination, exert differences with
                      regard to their interaction with ARTD10 in cells. Precisely,
                      while the macrodomains of murine Artd8 interacted with
                      ARTD10 in cells in a MARylation-dependent manner, the
                      macrodomains of human ARTD8 interacted with ARTD10
                      independent of its catalytic activity. Moreover, we show
                      that a combination of macro2 and macro3 of murine Artd8 was
                      recruited more efficiently to ARTD10 during co-localization
                      experiments compared to the single domains. Therefore,
                      murine Artd8 macrodomain constructs can serve as a tool to
                      evaluate intracellular ARTD10 auto-modification levels using
                      the described methods, while the human ARTD8 macrodomains
                      are less suited because of ADPr-independent binding to
                      ARTD10. Protocols for co-immunoprecipitation and
                      co-localization experiments are described in detail.},
      cin          = {IAS-5 / JSC},
      ddc          = {570},
      cid          = {I:(DE-Juel1)IAS-5-20120330 / I:(DE-Juel1)JSC-20090406},
      pnm          = {511 - Computational Science and Mathematical Methods
                      (POF3-511)},
      pid          = {G:(DE-HGF)POF3-511},
      typ          = {PUB:(DE-HGF)7},
      pubmed       = {pmid:30097860},
      UT           = {WOS:000454740000005},
      doi          = {10.1007/978-1-4939-8588-3_4},
      url          = {https://juser.fz-juelich.de/record/857534},
}