Beyond protein modification: the rise of non-canonical ADP-ribosylation.
ADP Ribose Transferases
/ chemistry
ADP-Ribosylation
/ physiology
Adenosine Diphosphate
/ metabolism
Guanosine
/ metabolism
N-Glycosyl Hydrolases
/ physiology
Poly(ADP-ribose) Polymerases
/ metabolism
Regulatory Sequences, Ribonucleic Acid
Signal Transduction
Structure-Activity Relationship
Thymidine
/ metabolism
Ubiquitin
/ metabolism
ADP-ribosylation
PARP
nucleic acids
protein modification
Journal
The Biochemical journal
ISSN: 1470-8728
Titre abrégé: Biochem J
Pays: England
ID NLM: 2984726R
Informations de publication
Date de publication:
17 02 2022
17 02 2022
Historique:
received:
18
11
2021
revised:
18
01
2022
accepted:
21
01
2022
entrez:
17
2
2022
pubmed:
18
2
2022
medline:
1
3
2022
Statut:
ppublish
Résumé
ADP-ribosylation has primarily been known as post-translational modification of proteins. As signalling strategy conserved in all domains of life, it modulates substrate activity, localisation, stability or interactions, thereby regulating a variety of cellular processes and microbial pathogenicity. Yet over the last years, there is increasing evidence of non-canonical forms of ADP-ribosylation that are catalysed by certain members of the ADP-ribosyltransferase family and go beyond traditional protein ADP-ribosylation signalling. New macromolecular targets such as nucleic acids and new ADP-ribose derivatives have been established, notably extending the repertoire of ADP-ribosylation signalling. Based on the physiological relevance known so far, non-canonical ADP-ribosylation deserves its recognition next to the traditional protein ADP-ribosylation modification and which we therefore review in the following.
Identifiants
pubmed: 35175282
pii: 230805
doi: 10.1042/BCJ20210280
pmc: PMC8883491
doi:
Substances chimiques
Regulatory Sequences, Ribonucleic Acid
0
Ubiquitin
0
Guanosine
12133JR80S
Adenosine Diphosphate
61D2G4IYVH
ADP Ribose Transferases
EC 2.4.2.-
Poly(ADP-ribose) Polymerases
EC 2.4.2.30
N-Glycosyl Hydrolases
EC 3.2.2.-
ADP-ribosylarginine hydrolase
EC 3.2.2.19
Thymidine
VC2W18DGKR
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
463-477Subventions
Organisme : Cancer Research UK
ID : C35050/ A22284
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 : Wellcome Trust
Pays : United Kingdom
Organisme : Wellcome Trust
ID : 101794
Pays : United Kingdom
Informations de copyright
© 2022 The Author(s).
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