The function and regulation of ADP-ribosylation in the DNA damage response.
ADP-ribosylation
DNA synthesis and repair
PARP
Journal
Biochemical Society transactions
ISSN: 1470-8752
Titre abrégé: Biochem Soc Trans
Pays: England
ID NLM: 7506897
Informations de publication
Date de publication:
28 06 2023
28 06 2023
Historique:
received:
13
03
2023
revised:
27
04
2023
accepted:
02
05
2023
medline:
29
6
2023
pubmed:
12
5
2023
entrez:
12
5
2023
Statut:
ppublish
Résumé
ADP-ribosylation is a post-translational modification involved in DNA damage response (DDR). In higher organisms it is synthesised by PARP 1-3, DNA strand break sensors. Recent advances have identified serine residues as the most common targets for ADP-ribosylation during DDR. To ADP-ribosylate serine, PARPs require an accessory factor, HPF1 which completes the catalytic domain. Through ADP-ribosylation, PARPs recruit a variety of factors to the break site and control their activities. However, the timely removal of ADP-ribosylation is also key for genome stability and is mostly performed by two hydrolases: PARG and ARH3. Here, we describe the key writers, readers and erasers of ADP-ribosylation and their contribution to the mounting of the DDR. We also discuss the use of PARP inhibitors in cancer therapy and the ways to tackle PARPi treatment resistance.
Identifiants
pubmed: 37171085
pii: 233042
doi: 10.1042/BST20220749
pmc: PMC10317172
doi:
Substances chimiques
Hydrolases
EC 3.-
Serine
452VLY9402
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
995-1008Subventions
Organisme : Wellcome Trust
ID : 210634
Pays : United Kingdom
Organisme : Wellcome Trust
ID : 223107
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
Organisme : Cancer Research UK
ID : BST00260.BV00.01
Pays : United Kingdom
Informations de copyright
© 2023 The Author(s).
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