ArticleNucleic acids research2009
Ionizing radiation-dependent and independent phosphorylation of the 32-kDa subunit of replication protein A during mitosis.
Article in Nucleic acids research, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.
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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.
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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
27 citing papers in PubMed, 43 citations in OpenAlex.
- Activation of Pol theta-mediated end joining begins during mitotic commitment.bioRxiv : the preprint server for biology · 2026Article
- Replication Stress in Cancer: Mechanistic Insights and Therapeutic Opportunities for Radiosensitization.Current issues in molecular biology · 2026Review
- Mechanism of RPA phosphocode priming and tuning by CDK1/WEE1 signaling circuit.Nature communications · 2025Article
- Review
- Article
- Murine polyomavirus DNA transitions through spatially distinct nuclear replication subdomains during infection.PLoS pathogens · 2020Article
- Radiation resistance of normal human astrocytes: the role of non-homologous end joining DNA repair activity.Journal of radiation research · 2019Article
- Paths from DNA damage and signaling to genome rearrangements via homologous recombination.Mutation research · 2017Review
- A phosphorylation-and-ubiquitylation circuitry driving ATR activation and homologous recombination.Nucleic acids research · 2017Article
- RPA-coated single-stranded DNA as a platform for post-translational modifications in the DNA damage response.Cell research · 2015Review
- DNA-damage response during mitosis induces whole-chromosome missegregation.Cancer discovery · 2014Article
- Polo-like kinase 3 regulates CtIP during DNA double-strand break repair in G1.The Journal of cell biology · 2014Article
- Interplay of DNA damage and cell cycle signaling at the level of human replication protein A.DNA repair · 2014Article
- PARG is dispensable for recovery from transient replicative stress but required to prevent detrimental accumulation of poly(ADP-ribose) upon prolonged replicative stress.Nucleic acids research · 2014Article
- Supervillin binding to myosin II and synergism with anillin are required for cytokinesis.Molecular biology of the cell · 2013Article
- DNA polymerase η modulates replication fork progression and DNA damage responses in platinum-treated human cells.Scientific reports · 2013Article
- Human single-stranded DNA binding proteins are essential for maintaining genomic stability.BMC molecular biology · 2013Review
- Rfa2 is specifically dephosphorylated by Pph3 in Candida albicans.The Biochemical journal · 2013Article
- Distinct roles for DNA-PK, ATM and ATR in RPA phosphorylation and checkpoint activation in response to replication stress.Nucleic acids research · 2012Article
- Cell cycle-dependent mobility of Cdc45 determined in vivo by fluorescence correlation spectroscopy.PloS one · 2012Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
5 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The human single-stranded DNA-binding protein, replication protein A (RPA), is regulated by the N-terminal phosphorylation of its 32-kDa subunit, RPA2. RPA2 is hyperphosphorylated in response to various DNA-damaging agents and also phosphorylated in a cell-cycle-dependent manner during S- and M-phase, primarily at two CDK consensus sites, S23 and S29. Here we generated two monoclonal phospho-specific antibodies directed against these CDK sites. These phospho-specific RPA2-(P)-S23 and RPA2-(P)-S29 antibodies recognized mitotically phosphorylated RPA2 with high specificity. In addition, the RPA2-(P)-S23 antibody recognized the S-phase-specific phosphorylation of RPA2, suggesting that during S-phase only S23 is phosphorylated, whereas during M-phase both CDK sites, S23 and S29, are phosphorylated. Immunofluorescence microscopy revealed that the mitotic phosphorylation of RPA2 starts at the onset of mitosis, and dephosphorylation occurs during late cytokinesis. In mitotic cells treated with ionizing radiation (IR), we observed a rapid hyperphosphorylation of RPA2 in addition to its mitotic phosphorylation at S23 and S29, associated with a significant change in the subcellular localization of RPA. Our data also indicate that the RPA2 hyperphosphorylation in response to IR is facilitated by the activity of both ATM and DNA-PK, and is associated with activation of the Chk2 pathway.
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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.