ATR Signaling Uncouples the Role of RAD51 Paralogs in Homologous Recombination and Replication Stress Response.


Journal

Cell reports
ISSN: 2211-1247
Titre abrégé: Cell Rep
Pays: United States
ID NLM: 101573691

Informations de publication

Date de publication:
15 10 2019
Historique:
received: 19 02 2019
revised: 31 07 2019
accepted: 04 09 2019
entrez: 17 10 2019
pubmed: 17 10 2019
medline: 19 8 2020
Statut: ppublish

Résumé

ATR kinase-mediated replication checkpoint is vital for genome maintenance following replication stress. Previously, we showed that XRCC2-RAD51D (DX2) sub-complex of RAD51 paralogs restrains active DNA synthesis during dNTP alterations, in a manner dependent on ATR-mediated phosphorylation of XRCC2. Here, we find that unrestrained fork progression in XRCC2 deficiency and phosphorylation defect causes replication-associated errors, subsequently resulting in genome-wide double-strand breaks (DSBs) and early activation of ATM signaling. Cells defective in XRCC2 phosphorylation exhibit ATM/ATR-mediated early activation of XRCC3 during perturbed replication, which facilitates recombination-mediated repair of the post-replicative DNA damage and thereby promotes cell viability. Collectively, our findings identify collaborative roles of RAD51 paralog complexes during replication stress and reveal their differential regulation by ATR signaling to promote cell survival and genome integrity.

Identifiants

pubmed: 31618626
pii: S2211-1247(19)31185-4
doi: 10.1016/j.celrep.2019.09.008
pii:
doi:

Substances chimiques

2-morpholin-4-yl-6-thianthren-1-yl-pyran-4-one 0
DNA-Binding Proteins 0
Morpholines 0
Pyrones 0
RNA, Small Interfering 0
X-ray repair cross complementing protein 3 0
XRCC2 protein, human 0
ATR protein, human EC 2.7.11.1
Ataxia Telangiectasia Mutated Proteins EC 2.7.11.1
RAD51 protein, human EC 2.7.7.-
Rad51 Recombinase EC 2.7.7.-
Hydroxyurea X6Q56QN5QC

Types de publication

Journal Article Research Support, Non-U.S. Gov't

Langues

eng

Sous-ensembles de citation

IM

Pagination

551-559.e4

Informations de copyright

Copyright © 2019 The Author(s). Published by Elsevier Inc. All rights reserved.

Auteurs

Sneha Saxena (S)

Department of Biochemistry, Indian Institute of Science, Bangalore-560012, India.

Suruchi Dixit (S)

Department of Biochemistry, Indian Institute of Science, Bangalore-560012, India.

Kumar Somyajit (K)

Department of Biochemistry, Indian Institute of Science, Bangalore-560012, India. Electronic address: kr.somyajit@cpr.ku.dk.

Ganesh Nagaraju (G)

Department of Biochemistry, Indian Institute of Science, Bangalore-560012, India. Electronic address: nganesh@iisc.ac.in.

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Classifications MeSH