Protein kinase ATR inhibits E3 ubiquitin ligase CRL4
ATR
CP: Molecular biology
DNA damage response
DNA replication stress
PRL1
TSO2
WEE1
ribonucleotide reductase
Journal
Cell reports
ISSN: 2211-1247
Titre abrégé: Cell Rep
Pays: United States
ID NLM: 101573691
Informations de publication
Date de publication:
25 07 2023
25 07 2023
Historique:
received:
13
10
2022
revised:
14
03
2023
accepted:
07
06
2023
medline:
31
7
2023
pubmed:
24
6
2023
entrez:
24
6
2023
Statut:
ppublish
Résumé
The protein kinase ATR is essential for replication stress responses in all eukaryotes. Ribonucleotide reductase (RNR) catalyzes the formation of deoxyribonucleotide (dNTP), the universal building block for DNA replication and repair. However, the relationship between ATR and RNR is not well understood. Here, we show that ATR promotes the protein stability of RNR in Arabidopsis. Through an activation tagging-based genetic screen, we found that overexpression of TSO2, a small subunit of RNR, partially suppresses the hypersensitivity of the atr mutant to replication stress. Biochemically, TSO2 interacts with PRL1, a central subunit of the Cullin4-based E3 ubiquitin ligase CRL4
Identifiants
pubmed: 37354461
pii: S2211-1247(23)00696-4
doi: 10.1016/j.celrep.2023.112685
pii:
doi:
Substances chimiques
Arabidopsis Proteins
0
Ataxia Telangiectasia Mutated Proteins
EC 2.7.11.1
ATR protein, Arabidopsis
EC 2.7.1.-
Ribonucleotide Reductases
EC 1.17.4.-
Ubiquitin-Protein Ligases
EC 2.3.2.27
PRL1 protein, plant
0
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
112685Informations de copyright
Copyright © 2023 The Author(s). Published by Elsevier Inc. All rights reserved.
Déclaration de conflit d'intérêts
Declaration of interests The authors declare no competing interests.