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- W3202772783 abstract "Abstract Despite the involvement of Poly(ADP-ribose) polymerase-1 (PARP1) in many important biological pathways, the target residues of PARP1-mediated ADP-ribosylation remain ambiguous. To explicate the ADP-ribosylation regulome, we analyze human cells depleted for key regulators of PARP1 activity, histone PARylation factor 1 (HPF1) and ADP-ribosylhydrolase 3 (ARH3). Using quantitative proteomics, we characterize 1,596 ADP-ribosylation sites, displaying up to 1000-fold regulation across the investigated knockout cells. We find that HPF1 and ARH3 inversely and homogenously regulate the serine ADP-ribosylome on a proteome-wide scale with consistent adherence to lysine-serine-motifs, suggesting that targeting is independent of HPF1 and ARH3. Notably, we do not detect an HPF1-dependent target residue switch from serine to glutamate/aspartate under the investigated conditions. Our data support the notion that serine ADP-ribosylation mainly exists as mono-ADP-ribosylation in cells, and reveal a remarkable degree of histone co-modification with serine ADP-ribosylation and other post-translational modifications." @default.
- W3202772783 created "2021-10-11" @default.
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- W3202772783 date "2021-10-08" @default.
- W3202772783 modified "2023-10-15" @default.
- W3202772783 title "The regulatory landscape of the human HPF1- and ARH3-dependent ADP-ribosylome" @default.
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- W3202772783 doi "https://doi.org/10.1038/s41467-021-26172-4" @default.
- W3202772783 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/8501107" @default.
- W3202772783 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/34625544" @default.
- W3202772783 hasPublicationYear "2021" @default.
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