The regulatory landscape of the human HPF1- and ARH3-dependent ADP-ribosylome.
ADP-Ribosylation
Adenosine Diphosphate
/ metabolism
Carrier Proteins
/ genetics
Cell Line, Tumor
DNA Damage
Gene Knockout Techniques
Glycoside Hydrolases
/ genetics
Histones
/ metabolism
Humans
Nuclear Proteins
/ genetics
Protein Processing, Post-Translational
Proteome
/ metabolism
Proteomics
Serine
/ metabolism
Journal
Nature communications
ISSN: 2041-1723
Titre abrégé: Nat Commun
Pays: England
ID NLM: 101528555
Informations de publication
Date de publication:
08 10 2021
08 10 2021
Historique:
received:
06
02
2021
accepted:
21
09
2021
entrez:
9
10
2021
pubmed:
10
10
2021
medline:
3
11
2021
Statut:
epublish
Résumé
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.
Identifiants
pubmed: 34625544
doi: 10.1038/s41467-021-26172-4
pii: 10.1038/s41467-021-26172-4
pmc: PMC8501107
doi:
Substances chimiques
Carrier Proteins
0
HPF1 protein, human
0
Histones
0
Nuclear Proteins
0
Proteome
0
Serine
452VLY9402
Adenosine Diphosphate
61D2G4IYVH
Glycoside Hydrolases
EC 3.2.1.-
ADPRS protein, human
EC 3.2.1.143
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
5893Subventions
Organisme : Wellcome Trust
ID : 101794
Pays : United Kingdom
Organisme : Wellcome Trust
ID : 210634
Pays : United Kingdom
Organisme : Biotechnology and Biological Sciences Research Council
ID : BB/R007195/1
Pays : United Kingdom
Organisme : Cancer Research UK
ID : C35050/A22284
Pays : United Kingdom
Informations de copyright
© 2021. The Author(s).
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