ReviewCell cycle (Georgetown, Tex.)2010
Phosphorylation-regulated binding of Ctp1 to Nbs1 is critical for repair of DNA double-strand breaks.
Review in Cell cycle (Georgetown, Tex.), 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers, 1 of them a synthesis that pooled it.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
20 citing papers in PubMed, 1 synthesis or guideline pooled it.
- Significant association between Nijmegen breakage syndrome 1 657del5 polymorphism and breast cancer risk.Tumour biology : the journal of the International Society for Oncodevelopmental Biology and Medicine · 2013Pooled it
- Targeting CK2-mediated phosphorylation of p53R2 sensitizes BRCA-proficient cancer cells to PARP inhibitors.Oncogene · 2023Article
- Hereditary Prostate Cancer: Genes Related, Target Therapy and Prevention.International journal of molecular sciences · 2021Review
- A conserved Ctp1/CtIP C-terminal peptide stimulates Mre11 endonuclease activity.Proceedings of the National Academy of Sciences of the United States of America · 2021Article
- Role of protein kinase CK2 in antitumor drug resistance.Journal of experimental & clinical cancer research : CR · 2019Review
- Exploiting DNA repair defects in colorectal cancer.Molecular oncology · 2019Review
- Two separable functions of Ctp1 in the early steps of meiotic DNA double-strand break repair.Nucleic acids research · 2015Article
- Functional Role of NBS1 in Radiation Damage Response and Translesion DNA Synthesis.Biomolecules · 2015Review
- Phosphorylation of Sae2 Mediates Forkhead-associated (FHA) Domain-specific Interaction and Regulates Its DNA Repair Function.The Journal of biological chemistry · 2015Article
- The Mre11/Rad50/Nbs1 complex: recent insights into catalytic activities and ATP-driven conformational changes.Experimental cell research · 2014Review
- Structural studies of DNA end detection and resection in homologous recombination.Cold Spring Harbor perspectives in biology · 2014Review
- Article
- DNA-dependent protein kinase regulates DNA end resection in concert with Mre11-Rad50-Nbs1 (MRN) and ataxia telangiectasia-mutated (ATM).The Journal of biological chemistry · 2013Article
- A mutation in the FHA domain of Coprinus cinereus Nbs1 Leads to Spo11-independent meiotic recombination and chromosome segregation.G3 (Bethesda, Md.) · 2013Article
- Brc1 links replication stress response and centromere function.Cell cycle (Georgetown, Tex.) · 2013Review
- Crosstalk between casein kinase II and Ste20-related kinase Nak1.Cell cycle (Georgetown, Tex.) · 2013Article
- End-resection at DNA double-strand breaks in the three domains of life.Biochemical Society transactions · 2013Review
- Regulation of DNA damage following termination of Hedgehog (HH) survival signaling at the level of the GLI genes in human colon cancer.Oncotarget · 2012Article
- Regulatory networks integrating cell cycle control with DNA damage checkpoints and double-strand break repair.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2011Review
- The MRN complex in double-strand break repair and telomere maintenance.FEBS letters · 2010Review
Corrections and comments
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Authors and funding
4 authors.
Funding
Abstract
Repair of DNA double-strand breaks (DSBs) is critical for cell survival and for maintaining genome stability in eukaryotes. In Schizosaccharomyces pombe, the Mre11-Rad50-Nbs1 (MRN) complex and Ctp1 cooperate to perform the initial steps that process and repair these DNA lesions via homologous recombination (HR). While Ctp1 is recruited to DSBs in an MRN-dependent manner, the specific mechanism of this process remained unclear. We recently found that Ctp1 is phosphorylated on a domain rich in putative Casein kinase 2 (CK2) phosphoacceptor sites that resembles the SDTD repeats of Mdc1. Furthermore, phosphorylation of this motif is required for interaction with the FHA domain of Nbs1 that localizes Ctp1 to DSB sites. Here, we review and discuss these findings, and we present new data that further characterize the cellular consequences of mutating CK2 phosphorylation motifs of Ctp1, including data showing that these sites are critical for meiosis.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.