title: Identification of ADP-ribosylated peptides and ADP-ribose acceptor sites.
abstract: ADP-ribosylation is a post-translational modification of proteins that comprises the transfer of the ADP-ribose moiety from NAD+ to specific amino acid residues on substrate proteins or to ADP-ribose itself. It is catalyzed by ADP-ribosyltransferases, a family of currently 22 human proteins that all possess an ADP-ribosyltransferase catalytic domain. ADP-ribosylation is a reversible modification that can be hydrolyzed by ADP-ribosylhydrolases. In order to define the functional role of cellular ADP-ribosylation and the functional contribution of distinct ARTD family members, it is necessary to identify all ADP-ribosylated proteins, as well as their modified residues in the context of different cellular conditions and stresses. Here, we summarize the most recent progress in defining the cellular ADP-ribosylome and the efforts to detect ADP-ribose acceptor sites by enzymatic reactions and mass-spectrometry.
authors.affiliation: Institute of Veterinary Biochemistry and Molecular Biology, University of Zurich, Switzerland.
authors.forename: Florian
authors.initials: F
authors.lastname: Rosenthal
authors.affiliation: Institute of Veterinary Biochemistry and Molecular Biology, University of Zurich, Switzerland.
authors.forename: Michael O
authors.initials: MO
authors.lastname: Hottiger
mesh_terms: D036002:ADP Ribose Transferases / Q000378:metabolism; D000246:Adenosine Diphosphate Ribose / Q000378:metabolism*; D000596:Amino Acids / Q000378:metabolism; D001665:Binding Sites; D006801:Humans; D009699:N-Glycosyl Hydrolases / Q000378:metabolism; D009243:NAD / Q000378:metabolism; D010455:Peptides / Q000378:metabolism*; D011499:Protein Processing, Post-Translational; D011506:Proteins / Q000737:chemistry / Q000378:metabolism*
chemical_list: D000596:Amino Acids; D010455:Peptides; D011506:Proteins; D009243:NAD; D000246:Adenosine Diphosphate Ribose; D036002:ADP Ribose Transferases; D009699:N-Glycosyl Hydrolases; C046422:ADP-ribosylarginine hydrolase