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ADP-ribosylation (ADPr) is a posttranslational modification (PTM) of proteins that controls many cellular processes, including DNA repair, transcription, chromatin regulation and mitosis. A number of proteins catalyse the transfer and hydrolysis of ADPr, and also specify how and when the modification is conjugated to the targets. We recently discovered a new form of ADPr that is attached to serine residues in target proteins (Ser-ADPr) and showed that this PTM is specifically made by PARP1/HPF1 and PARP2/HPF1 complexes. In this work, we found by quantitative proteomics that histone Ser-ADPr is reversible in cells during response to DNA damage. By screening for the hydrolase that is responsible for the reversal of Ser-ADPr, we identified ARH3/ADPRHL2 as capable of efficiently and specifically removing Ser-ADPr of histones and other proteins. We further showed that Ser-ADPr is a major PTM in cells after DNA damage and that this signalling is dependent on ARH3.

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ADP-ribose, ADP-ribosylation, ARH3, PARP, biochemistry, human, macrodomain, ADP-Ribosylation, Carrier Proteins, Cell Line, Tumor, Glycoside Hydrolases, Histones, Humans, Nuclear Proteins, Poly (ADP-Ribose) Polymerase-1, Poly(ADP-ribose) Polymerases, Protein Processing, Post-Translational, Proteome, Proteomics, Serine