ArticleNucleic acids research2018
Nuclear poly(A)-binding protein 1 is an ATM target and essential for DNA double-strand break repair.
Article in Nucleic acids research, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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Who cites it
13 citing papers in PubMed, 29 citations in OpenAlex.
- Article
- Nuclear poly(A)-binding protein and nucleolin utilize their RNA recognition motifs to read PAR chains.Nucleic acids research · 2025Article
- ZC3H4 safeguards genome integrity by preventing transcription-replication conflicts at noncoding RNA loci.Science advances · 2025Article
- Phosphorylation of the nuclear poly(A) binding protein (PABPN1) during mitosis protects mRNA from hyperadenylation and maintains transcriptome dynamics.Nucleic acids research · 2024Article
- Oculopharyngeal muscular dystrophy mutations link the RNA-binding protein HNRNPQ to autophagosome biogenesis.Aging cell · 2023Article
- PABPN1 regulates mRNA alternative polyadenylation to inhibit bladder cancer progression.Cell & bioscience · 2023Article
- Higher ATM expression in lymphoblastoid cell lines from centenarian compared with younger women.Drug development research · 2022Article
- Writing and Erasing O-GlcNAc on Casein Kinase 2 Alpha Alters the Phosphoproteome.ACS chemical biology · 2022Article
- Coordination of RNA Processing Regulation by Signal Transduction Pathways.Biomolecules · 2021Review
- Phosphoproteomics reveals novel modes of function and inter-relationships among PIKKs in response to genotoxic stress.The EMBO journal · 2021Article
- Integrative proteomics and phosphoproteomics in pulmonary arterial hypertension.Scientific reports · 2019Article
- EXOSC10 is required for RPA assembly and controlled DNA end resection at DNA double-strand breaks.Nature communications · 2019Article
- Beyond the Poly(A) Tail: The Expanding Functional Landscape of PABPN1 and Its Dysregulation in OPMD and Cancer.Wiley interdisciplinary reviews. RNAReview
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Authors and funding
11 authors at 3 institutions in 3 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The DNA damage response (DDR) is an extensive signaling network that is robustly mobilized by DNA double-strand breaks (DSBs). The primary transducer of the DSB response is the protein kinase, ataxia-telangiectasia, mutated (ATM). Here, we establish nuclear poly(A)-binding protein 1 (PABPN1) as a novel target of ATM and a crucial player in the DSB response. PABPN1 usually functions in regulation of RNA processing and stability. We establish that PABPN1 is recruited to the DDR as a critical regulator of DSB repair. A portion of PABPN1 relocalizes to DSB sites and is phosphorylated on Ser95 in an ATM-dependent manner. PABPN1 depletion sensitizes cells to DSB-inducing agents and prolongs the DSB-induced G2/M cell-cycle arrest, and DSB repair is hampered by PABPN1 depletion or elimination of its phosphorylation site. PABPN1 is required for optimal DSB repair via both nonhomologous end-joining (NHEJ) and homologous recombination repair (HRR), and specifically is essential for efficient DNA-end resection, an initial, key step in HRR. Using mass spectrometry analysis, we capture DNA damage-induced interactions of phospho-PABPN1, including well-established DDR players as well as other RNA metabolizing proteins. Our results uncover a novel ATM-dependent axis in the rapidly growing interface between RNA metabolism and the DDR.
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